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AMP + diphosphate + L-tyrosyl-tRNATyr
ATP + L-tyrosine + tRNATyr
-
-
-
-
?
ATP + 3-(2-naphthyl)alanine + tRNATyr
AMP + diphosphate + 3-(2-naphthyl)alanyl-tRNATyr
ATP + 3-(5-hydroxypyridin-2-yl)-L-alanine + tRNATyr
?
-
-
-
?
ATP + 3-amino-L-tyrosine + tRNATyr
AMP + 3-amino-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + 3-azido-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + diphosphate + 3-azido-L-tyrosyl-tRNATyr
ATP + 3-chloro-L-tyrosine + tRNATyr
AMP + 3-chloro-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + 3-iodo-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + diphosphate + 3-iodo-L-tyrosyl-tRNATyr
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
mutant Y73V/Q195C and other mutants, no activity with the wild-type enzyme
-
?
ATP + 3-methoxy-L-tyrosine + tRNATyr
AMP + 3-methoxy-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-nitro-L-tyrosine + tRNATyr
AMP + 3-nitro-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + 4-acetylphenylalanine + tRNATyr
AMP + diphosphate + 4-acetylphenylalanyl-tRNATyr
ATP + 4-bromophenylalanine + tRNATyr
AMP + diphosphate + 4-bromophenylalanyl-tRNATyr
ATP + D-3,4-dihydroxyphenylalanine + tRNATyr
AMP + D-3,4-dihydroxyphenylalanine-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + D-tyrosine + tRNATyr
AMP + D-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + D-tyrosine + tRNATyr
AMP + diphosphate + D-tyrosyl-tRNATyr
enzyme TyrRS has a detectable, natural activity for the D-tyrosine stereoisomer, only tenfold less than for L-Tyr
-
-
?
ATP + L-3,4-dihydroxyphenylalanine + tRNATyr
AMP + L-3,4-dihydroxyphenylalanine-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + L-beta-(5-hydroxy-2-pyridyl)-alanine + tRNATyr
AMP + L-beta-(5-hydroxy-2-pyridyl)-alanine-tRNATyr + diphosphate
ATP + L-tyrosine + native yeast tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
ATP + L-tyrosine + tRNATyr + A22G mutated tRNATyr transcript
?
-
-
-
-
?
ATP + L-tyrosine + tRNATyr + G15A mutated tRNATyr transcript
?
-
-
-
-
?
ATP + L-tyrosine + tRNATyr + U54C mutated tRNATyr transcript
?
-
-
-
-
?
ATP + L-tyrosine + tRNATyr(G34C)
AMP + diphosphate + L-tyrosyl-tRNATyr(G34C)
ATP + L-tyrosine + tRNATyr(wild-type)
AMP + diphosphate + L-tyrosyl-tRNATyr(wild-type)
ATP + L-tyrosine + tRNATyrGTA
AMP + diphosphate + L-tyrosyl-tRNATyrGTA
two sequences, tRNATyr1 and tRNATyr2, substrate CHO tRNATyrGTA is recombinantly expressed. CHOTyrRS is able to attach Phe to both tRNATyr2 and CHO total tRNA containing native tRNATyr, excluding the possibility that mischarging results from the lack of post-transcriptional modifications to the in vitro-transcribed substrate
-
-
?
ATP + m-fluoro-D,L-tyrosine + tRNATyr
AMP + m-fluoro-D,L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + N-acetyl-L-tyrosine + tRNATyr
AMP + N-acetyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + N-formyl-L-tyrosine + tRNATyr
AMP + N-formyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + N-o-nitrophenylsulfenyl-L-tyrosine + tRNATyr
AMP + N-o-nitrophenylsulfenyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + O-dansyl-L-tyrosine + tRNATyr
AMP + O-dansyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + O-methyl-L-tyrosine + tRNATyr
AMP + O-methyl-L-Tyr-tRNATyr + diphosphate
ATP + O-phospho-L-tyrosine + tRNATyr
AMP + O-phospho-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + p-acetyl-L-phenylalanine + tRNATyr
AMP + diphosphate + p-acetyl-L-phenylalanyl-tRNATyr
aminoacyl-tRNA synthetases are designed through a combination of homology modeling, molecular docking and binding affinity computation with the purpose of incorporating pACPhe into proteins in Escherichia coli
-
-
?
ATP + p-iodophenylalanine + tRNATyr
AMP + diphosphate + p-iodophenylalanyl-tRNATyr
-
a variant of the Methanococcus jannaschii tyrosyl synthetase that selectively incorporates para-iodophenylalanine in response to an amber stop codon is identified
-
-
?
ATP + tyrosine + tRNATyr
?
-
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
additional information
?
-
AMP + diphosphate
ATP
-
-
-
?
AMP + diphosphate
ATP
-
-
-
?
AMP + diphosphate
ATP
-
-
-
?
AMP + diphosphate
ATP
-
-
-
-
?
AMP + diphosphate
ATP
-
-
-
?
ATP + 3-(2-naphthyl)alanine + tRNATyr
AMP + diphosphate + 3-(2-naphthyl)alanyl-tRNATyr
activity of a natural mutant enzyme, NpAla TyrRS activity
-
-
?
ATP + 3-(2-naphthyl)alanine + tRNATyr
AMP + diphosphate + 3-(2-naphthyl)alanyl-tRNATyr
activity of a natural mutant enzyme, NpAla TyrRS activity, altered specificity is due to both side-chain and backbone rearrangements within the active site that modify hydrogen bonds and packing interactions with substrate, as well as disrupt the alpha8-helix, which spans the WT active site
-
-
?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + diphosphate + 3-azido-L-tyrosyl-tRNATyr
-
-
-
?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + diphosphate + 3-azido-L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + diphosphate + 3-azido-L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + diphosphate + 3-iodo-L-tyrosyl-tRNATyr
-
-
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + diphosphate + 3-iodo-L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + diphosphate + 3-iodo-L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + 4-acetylphenylalanine + tRNATyr
AMP + diphosphate + 4-acetylphenylalanyl-tRNATyr
activity of a natural mutant enzyme
-
-
?
ATP + 4-acetylphenylalanine + tRNATyr
AMP + diphosphate + 4-acetylphenylalanyl-tRNATyr
activity of a natural mutant enzyme, altered specificity is due to both side-chain and backbone rearrangements within the active site that modify hydrogen bonds and packing interactions with substrate, as well as disrupt the alpha8-helix, which spans the WT active site
-
-
?
ATP + 4-bromophenylalanine + tRNATyr
AMP + diphosphate + 4-bromophenylalanyl-tRNATyr
activity of a natural mutant enzyme, p-BrPhe TyrRS activity
-
-
?
ATP + 4-bromophenylalanine + tRNATyr
AMP + diphosphate + 4-bromophenylalanyl-tRNATyr
activity of a natural mutant enzyme, p-BrPhe TyrRS activity, altered specificity is due to both side-chain and backbone rearrangements within the active site that modify hydrogen bonds and packing interactions with substrate, as well as disrupt the alpha8-helix, which spans the WT active site
-
-
?
ATP + L-beta-(5-hydroxy-2-pyridyl)-alanine + tRNATyr
AMP + L-beta-(5-hydroxy-2-pyridyl)-alanine-tRNATyr + diphosphate
-
L-beta-(5-hydroxy-2-pyridyl)-alanine i.e. azatyrosine, mutant F130S, and wild-type enzyme the latter showing low activity
-
?
ATP + L-beta-(5-hydroxy-2-pyridyl)-alanine + tRNATyr
AMP + L-beta-(5-hydroxy-2-pyridyl)-alanine-tRNATyr + diphosphate
-
L-beta-(5-hydroxy-2-pyridyl)-alanine i.e. azatyrosine, mutant F130S shows 17fold higher activity in vivo than the wild-type enzyme
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
the TyrRS specificity for tyrosine and conformity with the identity rules for tRNATyr for archea/eukarya, anticodon binding site, overview
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
functional idiosyncrasies of the viral TyrRS, activity with Escherichia coli tRNATyr, Plasmodium falciparum tRNATyr, and diverse wild-type and mutant Saccharomyces cerevisiae tRNATyrs, overview, the TyrRS specificity for tyrosine and recognition of the tRNATyr acceptor stem show conformity with the identity rules for tRNATyr for archea/eukarya, anticodon binding site, overview
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
wild-type activity
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
identitification of determinants in the cognate tRNATyr, the tRNATyr molecule forms an L-shaped structure, the acceptor stem and anticodon loop of the tRNATyr interact with different subunits of the dimeric TyrRS molecule, overview
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
-
r
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
2-step reaction mechanism, 1. activation of the amino acid by MgATP2- to form an enzyme-bound aminoacyl-adenylate intermediate, 2. transfer of the amino acid to the 3'-end of its cognate tRNATyr
-
r
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
2-step reaction, 1. activation of L-tyrosine with ATP to form L-Tyr-AMP, 2. transfer of the tyrosyl-group to tRNATyr
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
the enzyme aminoacylates Escherichia coli tRNA as well as in vitro transcribed human mitochondrial tRNAs
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + L-tyrosine + tRNATyr(G34C)
AMP + diphosphate + L-tyrosyl-tRNATyr(G34C)
the enzyme strictly recognizes the C1-G72 base pair, whereas the enzyme from Thermus thermophilus recognizes the G1-C72 in a different manner using different residues
-
-
?
ATP + L-tyrosine + tRNATyr(G34C)
AMP + diphosphate + L-tyrosyl-tRNATyr(G34C)
the enzyme strictly recognizes the C1-G72 base pair, whereas the enzyme from Thermus thermophilus recognizes the G1-C72 in a different manner using different residues
-
-
?
ATP + L-tyrosine + tRNATyr(wild-type)
AMP + diphosphate + L-tyrosyl-tRNATyr(wild-type)
the enzyme strictly recognizes the C1-G72 base pair, whereas the enzyme from Thermus thermophilus recognizes the G1-C72 in a different manner using different residues
-
-
?
ATP + L-tyrosine + tRNATyr(wild-type)
AMP + diphosphate + L-tyrosyl-tRNATyr(wild-type)
the enzyme strictly recognizes the C1-G72 base pair, whereas the enzyme from Thermus thermophilus recognizes the G1-C72 in a different manner using different residues
-
-
?
ATP + O-methyl-L-tyrosine + tRNATyr
AMP + O-methyl-L-Tyr-tRNATyr + diphosphate
-
-
?
ATP + O-methyl-L-tyrosine + tRNATyr
AMP + O-methyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
K2ATP2- or Na2ATP2-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
r
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
same affinity for tRNA or tRNA acylated with tyrosine
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
Na2ATP2-, specific for tyrosine as amino acid
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
phosphorothioate analogs of ATP
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
2-step reaction mechanism, 1. activation of the amino acid by MgATP2- to form an enzyme-bound aminoacyl-adenylate intermediate, 2. transfer of the amino acid to the 3'-end of its cognate tRNATyr
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
2-step reaction: 1. tyrosine activation to form the tyrosinyl-adenylate intermediate, 2. transfer of tyrosine from the tyrosinyl-adenylate intermediate to the tRNATyr
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
extreme high fidelity in charging the tRNA with an amino acid
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
tRNATyr substrate from Escherichia coli
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
enzyme plays a key role in protein biosynthesis
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
specificity for amino acids, with regard to the specificity for ATP the hydroxy group of ribose and the amino group in position 6 of the base are essential
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
heterologous tRNATyr from Escherichia coli and Methanococcus jannashii, tyrosylation efficiency of tRNA variants: determinants are base pair C1-G72, discriminator residue A73, and the 3 anticodon bases G34, U35, and A36
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
extreme high fidelity in charging the tRNA with an amino acid
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
enzyme plays a key role in protein biosynthesis
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
tRNATyr structure requirements, the C-terminal domain has a crucial role in the recognition of tRNATyr, first by recognizing the tRNA's unique shape and secondly by participating in specific interactions with one of the anticodon bases
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
tRNATyr structure requirements, the C-terminal domain has a crucial role in the recognition of tRNATyr, first by recognizing the tRNA's unique shape and secondly by participating in specific interactions with one of the anticodon bases
-
?
additional information
?
-
mimivirus aminoacyl-tRNA synthetases function as regular translation enzymes in infected amoebas
-
-
?
additional information
?
-
-
no activity with 4-azido-L-phenylalanine, 4-amino-L-phenylalanine, 4-nitro-L-phenylalanine, 4-methyl-L-phenylalanine, 4-fluoro-L-phenylalanine, 4-chloro-L-phenylalanine, 4-bromo-L-phenylalanine
-
-
?
additional information
?
-
no activity with 4-azido-L-phenylalanine, 4-amino-L-phenylalanine, 4-nitro-L-phenylalanine, 4-methyl-L-phenylalanine, 4-fluoro-L-phenylalanine, 4-chloro-L-phenylalanine, 4-bromo-L-phenylalanine
-
-
?
additional information
?
-
-
conformational flexibility of cytokine-like C-module of the enzyme
-
-
?
additional information
?
-
the presence of the C-terminal EMAP II-domain has no effect on the recognition of cognate Tyr and discrimination against noncognate Phe
-
-
?
additional information
?
-
-
the presence of the C-terminal EMAP II-domain has no effect on the recognition of cognate Tyr and discrimination against noncognate Phe
-
-
?
additional information
?
-
residues Asp81, Tyr175, Gln179, and Gln201 coordinate the ammonium group of the L-Tyr ligand
-
-
?
additional information
?
-
-
residues Asp81, Tyr175, Gln179, and Gln201 coordinate the ammonium group of the L-Tyr ligand
-
-
?
additional information
?
-
-
the enzyme's C-terminal domain, an EMAP II-like protein, is active in angiogenesis pathways and stimulates immune cells, when cleaved off the enzyme, it stimulates blood vessel development
-
?
additional information
?
-
-
TyrRS deficiency is involved in the autosomal dominant intermediate Charcot-Marie-Tooth neuropathy type C disorder, overview
-
-
?
additional information
?
-
-
recombinant hTyrRS also synthesizes kyotorphin from tyrosine, arginine, and ATP, cf. EC 6.3.2.24
-
-
?
additional information
?
-
-
two distinct conformational states of the active site in the three Leishmania major TyrRS structures
-
-
?
additional information
?
-
high degree of structural plasticity that is observed in these aminoacyl-tRNA synthetases, overview
-
-
?
additional information
?
-
enzyme TyrRS has a detectable, natural, tRNA-acylation activity for the D-tyrosine stereoisomer, being capable of charging D-Tyr onto tRNATyr to form D-Tyr-tRNA instead of the usual L-Tyr-tRNA
-
-
?
additional information
?
-
-
enzyme TyrRS has a detectable, natural, tRNA-acylation activity for the D-tyrosine stereoisomer, being capable of charging D-Tyr onto tRNATyr to form D-Tyr-tRNA instead of the usual L-Tyr-tRNA
-
-
?
additional information
?
-
enzyme TyrRS has a detectable, natural, tRNA-acylation activity for the D-tyrosine stereoisomer, being capable of charging D-Tyr onto tRNATyr to form D-Tyr-tRNA instead of the usual L-Tyr-tRNA
-
-
?
additional information
?
-
enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr
-
-
?
additional information
?
-
-
enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr
-
-
?
additional information
?
-
enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr
-
-
?
additional information
?
-
-
CYT-18 protein is a tyrosyl-tRNA synthetase adapted to function in group I intron splicing by acquiring a new RNA binding surface
-
-
?
additional information
?
-
-
no activity with tRNAAsp and tRNAPhe
-
?
additional information
?
-
the lack of cross-reactivity between archaeal/eukaryotic and bacterial TyrRS-tRNATyr pairs most probably lies in the different sequence of the last base pair of the acceptor stem, C1-G72 vs G1-C72, of tRNATyr, the recognition mode of Tyr-AMP is conserved among the TyrRSs from the three kingdoms, overview
-
-
?
additional information
?
-
-
the lack of cross-reactivity between archaeal/eukaryotic and bacterial TyrRS-tRNATyr pairs most probably lies in the different sequence of the last base pair of the acceptor stem, C1-G72 vs G1-C72, of tRNATyr, the recognition mode of Tyr-AMP is conserved among the TyrRSs from the three kingdoms, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + 3-(2-naphthyl)alanine + tRNATyr
AMP + diphosphate + 3-(2-naphthyl)alanyl-tRNATyr
activity of a natural mutant enzyme, NpAla TyrRS activity
-
-
?
ATP + 4-acetylphenylalanine + tRNATyr
AMP + diphosphate + 4-acetylphenylalanyl-tRNATyr
activity of a natural mutant enzyme
-
-
?
ATP + 4-bromophenylalanine + tRNATyr
AMP + diphosphate + 4-bromophenylalanyl-tRNATyr
activity of a natural mutant enzyme, p-BrPhe TyrRS activity
-
-
?
ATP + L-beta-(5-hydroxy-2-pyridyl)-alanine + tRNATyr
AMP + L-beta-(5-hydroxy-2-pyridyl)-alanine-tRNATyr + diphosphate
-
L-beta-(5-hydroxy-2-pyridyl)-alanine i.e. azatyrosine, mutant F130S shows 17fold higher activity in vivo than the wild-type enzyme
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
ATP + tyrosine + tRNATyr
?
-
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
additional information
?
-
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
the TyrRS specificity for tyrosine and conformity with the identity rules for tRNATyr for archea/eukarya, anticodon binding site, overview
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
wild-type activity
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
-
r
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
enzyme plays a key role in protein biosynthesis
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
enzyme plays a key role in protein biosynthesis
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
additional information
?
-
mimivirus aminoacyl-tRNA synthetases function as regular translation enzymes in infected amoebas
-
-
?
additional information
?
-
-
the enzyme's C-terminal domain, an EMAP II-like protein, is active in angiogenesis pathways and stimulates immune cells, when cleaved off the enzyme, it stimulates blood vessel development
-
?
additional information
?
-
-
TyrRS deficiency is involved in the autosomal dominant intermediate Charcot-Marie-Tooth neuropathy type C disorder, overview
-
-
?
additional information
?
-
enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr
-
-
?
additional information
?
-
-
enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr
-
-
?
additional information
?
-
enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr
-
-
?
additional information
?
-
-
CYT-18 protein is a tyrosyl-tRNA synthetase adapted to function in group I intron splicing by acquiring a new RNA binding surface
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-(3,4-dichlorophenyl)-4-(2-(4-methylpiperazin-1-yl)ethoxy)furan-2(5H)-one
-
-
3-(3,4-difluorophenyl)-4-(2-(piperidin-1-yl)ethoxy)furan-2(5H)-one
-
-
3-(3,4-dimethoxyphenyl)-4-(2-(4-methylpiperazin-1-yl)ethoxy)furan-2(5H)-one
-
-
3-(3,4-dimethoxyphenyl)-4-(2-(piperidin-1-yl)ethoxy)furan-2(5H)-one
-
-
3-(3-bromophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-(3-chlorophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-(3-hydroxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-(3-methoxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-(4-bromophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-(4-chlorophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-(4-hydroxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
replacement of the morpholine-ring in the side chain of the compound with a substituent containing more hydrophilic groups is probably more suitable for further modification. Most potent agent against Staphylococcus aureus ATCC 25923 with MIC50 value of 0.00023 mg/ml
3-(4-methoxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-phenyl-4-(2-(piperidin-1-yl)ethoxy)furan-2(5H)-one
-
-
3-phenyl-4-(2-(propylamino)ethoxy)furan-2(5H)-one
-
-
3-phenyl-4-(2-(pyrrolidin-1-yl)ethoxy)furan-2(5H)-one
-
-
3-phenyl-4-(phenylamino)furan-2(5H)-one
-
-
4-(2-(2,4-dichlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(2,4-dihydroxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(2,5-dichlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(2-(4-nitrophenyl)hydrazinyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(2-chlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(2-hydroxyphenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(2-methoxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(2-methylphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(2-nitrophenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(3,4-dichlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(3,4-dihydroxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(3,4-dimethoxyphenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(3,5-dihydroxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(3-bromophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
4-(2-(3-chlorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
4-(2-(3-chlorophenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(3-chlorophenylformyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
4-(2-(3-methylphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(3-nitrophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(3-pyridylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(3-trifluoromethylphenylformyoxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(4-bromophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
4-(2-(4-bromophenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(4-chlorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
4-(2-(4-chlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(4-fluorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
4-(2-(4-fluorophenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(4-fluorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(4-hydroxyphenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
4-(2-(4-hydroxyphenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(4-hydroxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(4-methylphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(4-methylpiperazin-1-yl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(4-nitrophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(6-hydroxynaphthalen-2-ylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(benzylamino)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(butylamino)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(cyclohexylamino)ethoxy)-3-(3,4-dimethoxyphenyl)furan-2(5H)-one
-
-
4-(2-(cyclohexylamino)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(naphthalen-2-ylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-butyryloxyethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-hexanoyloxyethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-morpholinoethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-octanoyloxyethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-phenylacetyloxylethoxy)-3-phenylfuran-2(5H)-one
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-bromobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-chlorobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-chloropyridine-3-carboxylate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-fluorobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-methoxybenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-methylbenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-nitrobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-(3-methylphenyl)propanoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-(4-methylphenyl)propanoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-aminobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-bromobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-chlorobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-fluorobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-hydroxybenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-methylbenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-phenylpropanoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-aminobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-bromobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-chlorobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-fluorobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-hydroxybenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-methylbenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 6-chloropyridine-3-carboxylate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 6-hydroxypyridine-3-carboxylate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl benzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl pyridine-3-carboxylate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl pyridine-4-carboxylate
-
-
5'-O-[N-(L-tyrosyl)sulfamoyl]adenosine
-
i.e. TyrSA, a tyrosyl adenylate analogue,. TyrSA is engaged in many interactions with active site residues occupying the tyrosine and adenine binding pockets. Residues making hydrogen bonds with the TyrSA tyrosyl group in the tyrosine binding pocket (YBP) are Y36, Y163, Q167, D170 and Q185. Residues G38, A72 and F75 are responsible for the hydrophobic interactions between enzyme and tyrosine moiety in the YBP
6-Aminomethyladenosine triphosphate
-
-
epigallocatechin gallate
strong inhibition
kaempferide
strong inhibition
L-tyrosinyl 1,4-anhydro-D-ribitol-5-O-phosphate
L-tyrosinyl 1-beta-naphthyl-1,4-anhydro-D-ribitol-5-O-phosphate
L-tyrosinyl N6-benzoyl adenylate
-
-
L-tyrosinyl uridine-5'-O-phosphate
L-tyrosinyl-2',3'-O-isopropylidene adenylate
L-tyrosinyl-2'-deoxy adenylate
L-tyrosinyl-3'-deoxy adenylate
N-(2-chlorophenyl)-N2-(phenylacetyl)glycinamide
-
-
N-(3,5-dichlorophenyl)-N2-(phenylacetyl)glycinamide
-
-
N-(3,5-difluorophenyl)-N2-(phenylacetyl)glycinamide
-
-
N-(3,5-dimethoxyphenyl)-N2-(phenylacetyl)glycinamide
-
-
N-(3-chlorophenyl)-N2-(phenylacetyl)glycinamide
-
-
N-(3-nitrophenyl)-N2-(phenylacetyl)glycinamide
-
-
N-(4-bromophenyl)-N2-(phenylacetyl)glycinamide
-
-
N-(4-bromophenyl)-N2-[(2-chlorophenyl)acetyl]glycinamide
-
-
N-(4-bromophenyl)-N2-[(3-bromophenyl)acetyl]glycinamide
-
-
N-(4-bromophenyl)-N2-[(3-chlorophenyl)acetyl]glycinamide
-
-
N-(4-chlorophenyl)-N2-(phenylacetyl)glycinamide
-
-
N-(4-methoxyphenyl)-N2-(phenylacetyl)glycinamide
-
-
N-(4-nitrophenyl)-N2-(phenylacetyl)glycinamide
-
-
N-phenyl-N2-(phenylacetyl)glycinamide
-
-
N2-[(2-chlorophenyl)acetyl]-N-(4-methoxyphenyl)glycinamide
-
-
N2-[(2-chlorophenyl)acetyl]-N-(4-nitrophenyl)glycinamide
-
-
N2-[(2-hydroxyphenyl)acetyl]-N-(4-methoxyphenyl)glycinamide
-
-
N2-[(3,4-dimethoxyphenyl)acetyl]-N-(4-methoxyphenyl)glycinamide
-
-
N2-[(3,4-dimethoxyphenyl)acetyl]-N-(4-nitrophenyl)glycinamide
-
-
N2-[(3-chlorophenyl)acetyl]-N-(4-methoxyphenyl)glycinamide
-
-
N2-[(3-chlorophenyl)acetyl]-N-(4-methylphenyl)glycinamide
-
-
N2-[(3-chlorophenyl)acetyl]-N-(4-nitrophenyl)glycinamide
-
-
N2-[(3-fluorophenyl)acetyl]-N-(4-methoxyphenyl)glycinamide
-
-
N2-[(3-fluorophenyl)acetyl]-N-(4-nitrophenyl)glycinamide
-
-
N2-[(3-hydroxyphenyl)acetyl]-N-(4-methoxyphenyl)glycinamide
-
-
N2-[(3-hydroxyphenyl)acetyl]-N-(4-nitrophenyl)glycinamide
-
-
N2-[(4-chlorophenyl)acetyl]-N-(3,5-dichlorophenyl)glycinamide
-
-
N2-[(4-chlorophenyl)acetyl]-N-(4-methoxyphenyl)glycinamide
-
-
N2-[(4-fluorophenyl)acetyl]-N-(4-methoxyphenyl)glycinamide
-
-
N2-[(4-fluorophenyl)acetyl]-N-(4-nitrophenyl)glycinamide
-
-
N2-[(4-hydroxyphenyl)acetyl]-N-(4-methoxyphenyl)glycinamide
-
-
N2-[(4-hydroxyphenyl)acetyl]-N-(4-nitrophenyl)glycinamide
-
-
N2-[(4-methylphenyl)acetyl]-N-(4-nitrophenyl)glycinamide
-
-
O-(adenosine-5'-O-yl) N-(L-tyrosyl)phosphoramidate
i.e. Tyr-AMPN, a non-hydrolyzable Tyr-AMP analog, binding structure, overview
resveratrol
inhibits the enzyme activity and the growth of promastigotes
tyrosinol
-
binding structure, overview
tyrosyl aryl dipeptides
-
inhibitor interacts with and occupies the key catalytic residues in the tyrosyl binding pocket of the catalytic site
acacetin
strong inhibition
acacetin
strong inhibition
acacetin
-
strong inhibition
AMP
-
inhibition is weakened by chloride
AMP
-
inhibition is weakened by chloride
chloride
-
inhibition in presence of 1 mM free Mg2+, no inhibition in presence of 10 mM free Mg2+
chloride
-
inhibition in presence of 1 mM free Mg2+, no inhibition in presence of 10 mM free Mg2+
chrysin
strong inhibition
chrysin
strong inhibition
chrysin
-
strong inhibition
diphosphate
-
inhibition is strengthened by chloride
diphosphate
-
inhibition is strengthened by chloride
fisetin
-
-
fisetin
inhibits the enzyme activity and the growth of promastigotes
fisetin
-
binding structure, overview
L-tyrosinyl 1,4-anhydro-D-ribitol-5-O-phosphate
-
-
L-tyrosinyl 1,4-anhydro-D-ribitol-5-O-phosphate
-
-
L-tyrosinyl 1-beta-naphthyl-1,4-anhydro-D-ribitol-5-O-phosphate
-
-
L-tyrosinyl 1-beta-naphthyl-1,4-anhydro-D-ribitol-5-O-phosphate
-
-
L-tyrosinyl uridine-5'-O-phosphate
-
25% inhibition at 0.1 mM
L-tyrosinyl uridine-5'-O-phosphate
-
-
L-tyrosinyl-2',3'-O-isopropylidene adenylate
-
-
L-tyrosinyl-2',3'-O-isopropylidene adenylate
-
-
L-tyrosinyl-2'-deoxy adenylate
-
-
L-tyrosinyl-2'-deoxy adenylate
-
-
L-tyrosinyl-3'-deoxy adenylate
-
-
L-tyrosinyl-3'-deoxy adenylate
-
-
PCMB
-
-
sulfate
-
inhibition in presence of 1 mM free Mg2+
sulfate
-
inhibition in presence of 1 mM free Mg2+
tyrosinyl adenylate
-
-
additional information
-
no inhibition by acetate up to 200 mM in presence of 1 mM free Mg2+
-
additional information
natural compounds as inhibitors of tyrosyl-tRNA synthetase, effects of various polyphenols, alkaloids, and terpenes-secondary metabolites produced by higher plants, overview. Most of them act as competitive inhibitors. Structure-activity relationship shows that the most potent flavonoid inhibitors contain hydroxyl group at position 5 and 7 of A ring and a -OCH3 group at position 4' of B ring
-
additional information
-
natural compounds as inhibitors of tyrosyl-tRNA synthetase, effects of various polyphenols, alkaloids, and terpenes-secondary metabolites produced by higher plants, overview. Most of them act as competitive inhibitors. Structure-activity relationship shows that the most potent flavonoid inhibitors contain hydroxyl group at position 5 and 7 of A ring and a -OCH3 group at position 4' of B ring
-
additional information
-
LdTyrRS specific nanobodies are generated in Lama glama. Nanobodies are the variable domains of camelid heavy chain-only antibodies. The nanobody NbA makes numerous crystal contacts and in addition reduces the flexibility of a loop of LdTyrRS. NbA is cloned in the pMESy4 vector that carries the pelB sequence coding for the secretion signal peptide of PelB and is expressed as His-tagged protein in Escherichia coli for subsequent purification from the bacterial periplasm by affinity chromatography and gel filtration. 4 anti-LdTyrRS nanobodies are tested as crystallization chaperones, crystallization and structure analysis and modeling, overview
-
additional information
natural compounds as inhibitors of tyrosyl-tRNA synthetase, effects of various polyphenols, alkaloids, and terpenes-secondary metabolites produced by higher plants, overview. Most of them act as competitive inhibitors. Structure-activity relationship shows that the most potent flavonoid inhibitors contain hydroxyl group at position 5 and 7 of A ring and a -OCH3 group at position 4' of B ring
-
additional information
-
natural compounds as inhibitors of tyrosyl-tRNA synthetase, effects of various polyphenols, alkaloids, and terpenes-secondary metabolites produced by higher plants, overview. Most of them act as competitive inhibitors. Structure-activity relationship shows that the most potent flavonoid inhibitors contain hydroxyl group at position 5 and 7 of A ring and a -OCH3 group at position 4' of B ring
-
additional information
-
no inhibition by L-tyrosinyl 1-beta-(E)-(3-ethoxycarbonyl-2-methylprop-2-enyl)-1,4-anhydro-D-ribitol-5-O-phosphate, N-(L-tyrosinyl)-N'-(5'-deoxy-5'-adenosinyl)-sulfamide, and 2(S)-amino-3-(4-hydroxyphenyl)propyl 1-(adenine-9-yl)-(E)-5,6-dideoxy-beta-D-ribohept-5-enfuranuronate hydrochloride
-
additional information
-
enzyme-inhibitor complexes
-
additional information
-
synthesis of a series of novel 4-alkoxy-3-arylfuran-2(5H)-ones as tyrosyl-tRNA synthetase inhibitors, binding model and structure-activity relationship, MIC50 values, overview
-
additional information
-
synthesis and evaluation of new tyrosyl-tRNA synthetase inhibitors as antibacterial agents based on a N2-(arylacetyl)glycinanilide scaffold, molecular docking study, antimicrobial activity, overview
-
additional information
-
synthesis and evaluation of a series of novel 4-hydroxy-3-(naphthalen-1-ylmethyl)thiophen-2(5H)-ones as tyrosyl-tRNA synthetase inhibitors, molecular docking, structure-activity relationships, overview
-
additional information
-
natural compounds as inhibitors of tyrosyl-tRNA synthetase, effects of various polyphenols, alkaloids, and terpenes-secondary metabolites produced by higher plants, overview. Most of them act as competitive inhibitors. Structure-activity relationship shows that the most potent flavonoid inhibitors contain hydroxyl group at position 5 and 7 of A ring and a -OCH3 group at position 4' of B ring
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2.04 - 2.43
3-chloro-L-tyrosine
0.625 - 1.3
3-fluoro-D,L-tyrosine
0.13 - 1.15
3-iodo-L-tyrosine
1.6
A22G mutated tRNATyr transcript
-
-
-
0.8
G15A mutated tRNATyr transcript
-
-
-
0.56 - 1.84
L-3,4-dihydroxyphenylalanine
0.018 - 0.038
L-beta-(5-hydroxy-2-pyridyl)-alanine
0.0002
L-tyrosyl-tRNATyr
-
deacylation
0.002
native yeast tRNATyr
-
pH 7.5, 30°C
-
0.00068 - 0.039
tRNATyr(G34C)
-
0.00035 - 0.0014
tRNATyr(wild-type)
-
2.2
U54C mutated tRNATyr transcript
-
-
-
additional information
additional information
-
2.04
3-chloro-L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme
2.43
3-chloro-L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
0.625
3-fluoro-D,L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme
1.3
3-fluoro-D,L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
0.13
3-iodo-L-tyrosine
-
pH 7.6, 37°C, mutant Y73V/Q195C
1.15
3-iodo-L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
0.00043
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant wild-type enzyme
0.00045
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 144AcK
0.00049
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK
0.00071
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK
0.00223
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK
0.07
ATP
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
0.13
ATP
-
aminoacylation reaction, pH 8.0, wild-type enzyme
0.217
ATP
-
ATP-diphosphate exchange reaction
0.5
ATP
-
ATP-diphosphate exchange reaction
1.7
ATP
-
ATP-diphosphate exchange reaction
2
ATP
-
mutant M55L, pH 7.8, 25°C
2.1
ATP
-
wild-type enzyme, pH 7.8, 25°C
2.4
ATP
-
mutant I52L, pH 7.8, 25°C
2.7
ATP
-
mutant L105V, pH 7.8, 25°C
3
ATP
-
pH 7.5, 25°C, mutant S225A and mutant K231A
4
ATP
-
pH 7.5, 25°C, wild-type enzyme and mutant S224A
4.1
ATP
-
pH 7.5, 25°C, mutant S226A
0.46
D-tyrosine
-
pH 7.6, 30°C, wild-type enzyme
14
D-tyrosine
-
pH 7.6, 30°C, mutant Y43G
22
K+
-
pH 7.5, 25°C, mutant S226A
24
K+
-
pH 7.5, 25°C, mutant S224A
30
K+
-
pH 7.5, 25°C, mutant S225A
32
K+
-
pH 7.5, 25°C, wild-type enzyme
0.56
L-3,4-dihydroxyphenylalanine
-
pH 7.6, 30°C, mutant Y43G
1.84
L-3,4-dihydroxyphenylalanine
-
pH 7.6, 30°C, wild-type enzyme
0.018
L-beta-(5-hydroxy-2-pyridyl)-alanine
-
wild-type enzyme, pH 7.5, 30°C
0.038
L-beta-(5-hydroxy-2-pyridyl)-alanine
-
mutant F130S, pH 7.5, 30°C
0.0003
L-tyrosine
-
30°C, purified recombinant His-tagged enzyme
0.0014
L-tyrosine
-
mutant M55L, pH 7.8, 25°C
0.0015
L-tyrosine
-
mutant TyrRS, KMGCA
0.0018
L-tyrosine
-
mutant I52L, pH 7.8, 25°C
0.0021
L-tyrosine
-
wild-type enzyme and mutant L105V, pH 7.8, 25°C
0.0033
L-tyrosine
-
wild-type enzyme, pH 7.5, 30°C
0.0043
L-tyrosine
-
mutant TyrRS, RMSSS
0.0043
L-tyrosine
-
wild-type TyrRS, KMSSS
0.0044
L-tyrosine
-
mutant TyrRS, AMSSS
0.0049
L-tyrosine
-
chloroplasts
0.0053
L-tyrosine
-
pH 7.6, 37°C, wild-type enzyme
0.00669
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK
0.00678
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK
0.0068
L-tyrosine
-
cytoplasm
0.00713
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant wild-type enzyme
0.00728
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 144AcK
0.00845
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK
0.012
L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme, radioisotopic assay
0.014
L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme, spectrophotometric assay
0.021
L-tyrosine
-
pH 7.5, 25°C, mutant S225A
0.021
L-tyrosine
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
0.027
L-tyrosine
-
aminoacylation reaction, pH 8.0, wild-type enzyme
0.03
L-tyrosine
-
pH 7.5, 25°C, mutant K231A
0.034
L-tyrosine
-
pH 7.5, 25°C, wild-type enzyme
0.042
L-tyrosine
-
pH 7.5, 25°C, mutant S226A
0.05
L-tyrosine
-
pH 7.5, 25°C, mutant S224A
0.066
L-tyrosine
-
mutant F130S, pH 7.5, 30°C
0.14
L-tyrosine
-
pH 7.6, 37°C, mutant Y73V/Q195C
0.146
L-tyrosine
recombinant wild-type enzyme, pH 7.8, 25°C
0.16
L-tyrosine
recombinant truncated mutant enzyme, pH 7.8, 25°C
1.19
L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
0.000022
tRNATyr
-
chloroplasts
0.000022
tRNATyr
-
in absence of KCl, pH 7.4, 30°C
0.000037
tRNATyr
-
in presence of 50 mM KCl, pH 7.4, 30°C
0.0000898
tRNATyr
-
cytoplasm
0.000093
tRNATyr
-
in presence of 100 mM KCl, pH 7.4, 30°C
0.00022
tRNATyr
55°C, pH 8.0
0.00022
tRNATyr
wild type enzyme, at 55°C, in 100 mM HEPES-NaOH (pH 8.0), 10 mM MgCl2, 10 mM KCl
0.00024
tRNATyr
-
in presence of 150 mM KCl, pH 7.4, 30°C
0.00037
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant wild-type enzyme
0.00042
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 144AcK
0.00045
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 85AcK
0.00048
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 355AcK
0.00052
tRNATyr
-
acylation
0.00052
tRNATyr
pH 7.6, 37°C, native Escherichia coli tRNATyr
0.0009
tRNATyr
-
30°C, purified recombinant His-tagged enzyme
0.0025
tRNATyr
-
aminoacylation reaction, pH 8.0, wild-type enzyme
0.0048
tRNATyr
pH 7.6, 37°C, human mitochondrial tRNATyr
0.00068
tRNATyr(G34C)
37°C, pH 7.5, mutant enzyme D268R
-
0.039
tRNATyr(G34C)
37°C, pH 7.5, wild-type enzyme
-
0.00035
tRNATyr(wild-type)
37°C, pH 7.5, wild-type enzyme
-
0.0014
tRNATyr(wild-type)
37°C, pH 7.5, mutant enzyme D268R
-
0.002
tyrosine
-
-
0.008
tyrosine
-
acylation
0.012
tyrosine
-
ATP-diphosphate exchange reaction
0.013
tyrosine
-
ATP-diphosphate exchange reaction and aminoacylation
additional information
additional information
-
-
-
additional information
additional information
-
role of a mobile loop, corresponding to KMSKS signature sequence in catalytic mechanism
-
additional information
additional information
-
role of threonine 234 in catalysis
-
additional information
additional information
-
kinetic analysis of mutation
-
additional information
additional information
-
role of lysine 233 in catalysis
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
stoichiometry of substrate binding
-
additional information
additional information
-
values for mutant strains
-
additional information
additional information
-
mutants
-
additional information
additional information
-
energy profiles for wild-type and mutant enzymes, kinetics for the second reaction step: wild-type enzyme and mutants D78A, Y169A, Q173A, D194A, and Q195A, kinetics for the first reaction step: wild-type enzyme, and mutants D194A and Q195A
-
additional information
additional information
-
fluorescence emission measurement for determination of steady-state kinetics for the His-tagged and the non-His-tagged recombinant enzyme
-
additional information
additional information
-
kinetics, influence of assay conditions, Km for diverse tRNA variants, overview
-
additional information
additional information
-
the C-terminal His-tag of the recombinant enzyme has little effect on the catalytic activity
-
additional information
additional information
kinetics with Escherichia coli tRNATyr, Plasmodium falciparum tRNATyr, and diverse wild-type and mutant Saccharomyces cerevisiae tRNATyrs, overview
-
additional information
additional information
-
kinetic parameters for anticodon mutants of tRNATyr and for for acceptor stem mutants of tRNATyr
-
additional information
additional information
kinetic parameters for anticodon mutants of tRNATyr and for for acceptor stem mutants of tRNATyr
-
additional information
additional information
calculation of the L-Tyr/D-Tyr binding free energy difference. Michaelis-Menten kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
calculation of the L-Tyr/D-Tyr binding free energy difference. Michaelis-Menten kinetics of wild-type and mutant enzymes
-
additional information
additional information
Michaelis-Menten steady-state kinetics. Steady-state kinetic constants for ATP-[32P]PPi exchange for CHO cytosolic full length wild-type and variant TyrRS
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics. Steady-state kinetic constants for ATP-[32P]PPi exchange for CHO cytosolic full length wild-type and variant TyrRS
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.13 - 6.08
3-chloro-L-tyrosine
0.62 - 6.08
3-fluoro-D,L-tyrosine
0.43 - 0.48
3-iodo-L-tyrosine
0.00003
A22G mutated tRNATyr transcript
-
-
-
0.0002
G15A mutated tRNATyr transcript
-
-
-
0.67 - 6.08
L-3,4-dihydroxyphenylalanine
0.042 - 0.11
L-beta-(5-hydroxy-2-pyridyl)-alanine
1.5
native yeast tRNATyr
-
pH 7.5, 30°C
-
0.07 - 0.079
tRNATyr(G34C)
-
0.12 - 0.19
tRNATyr(wild-type)
-
0.012
U54C mutated tRNATyr transcript
-
-
-
additional information
additional information
-
0.13
3-chloro-L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme
1.46
3-chloro-L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
6.08
3-chloro-L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
0.62
3-fluoro-D,L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
3.3
3-fluoro-D,L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme
4.96
3-fluoro-D,L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme
6.08
3-fluoro-D,L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
0.43
3-iodo-L-tyrosine
-
pH 7.6, 37°C, mutant Y73V/Q195C
0.48
3-iodo-L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
0.1
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK
2
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK
3.3
ATP
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
4.6
ATP
-
mutant M55L, pH 7.8, 25°C
5.29
ATP
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
6.8
ATP
-
mutant I52L, pH 7.8, 25°C
7.7
ATP
-
aminoacylation reaction, pH 8.0, wild-type enzyme
7.7
ATP
-
wild-type enzyme, pH 7.8, 25°C
11.9
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK
12
ATP
-
mutant L105V, pH 7.8, 25°C
12.3
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 144AcK
14.2
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant wild-type enzyme
0.37
D-tyrosine
-
pH 7.6, 30°C, mutant Y43G
1.2
D-tyrosine
-
pH 7.6, 30°C, wild-type enzyme
0.67
L-3,4-dihydroxyphenylalanine
-
pH 7.6, 30°C, mutant Y43G
1.65
L-3,4-dihydroxyphenylalanine
-
pH 7.6, 30°C, wild-type enzyme
6.08
L-3,4-dihydroxyphenylalanine
-
pH 7.6, 30°C, mutant Y43G
0.042
L-beta-(5-hydroxy-2-pyridyl)-alanine
-
mutant F130S, pH 7.5, 30°C
0.11
L-beta-(5-hydroxy-2-pyridyl)-alanine
-
wild-type enzyme, pH 7.5, 30°C
0.01
L-tyrosine
-
mutant TyrRS, RMSSS
0.012
L-tyrosine
-
mutant TyrRS, AMSSS
0.025
L-tyrosine
-
mutant TyrRS, KMGCA
0.045
L-tyrosine
-
pH 7.6, 37°C, mutant Y73V/Q195C
0.1
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK
0.53
L-tyrosine
-
wild-type TyrRS, KMSSS
0.74
L-tyrosine
-
wild-type enzyme, pH 7.5, 30°C
0.78
L-tyrosine
-
pH 7.5, 25°C, mutant S226A
0.95
L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
1.4
L-tyrosine
-
mutant F130S, pH 7.5, 30°C
1.49
L-tyrosine
-
30°C, purified recombinant His-tagged enzyme
2
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK
2.5
L-tyrosine
-
mutant M55L, pH 7.8, 25°C
3.3
L-tyrosine
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
3.6
L-tyrosine
-
mutant I52L, pH 7.8, 25°C
4.4
L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme, radioisotopic assay
4.6
L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme, spectrophotometric assay
4.9
L-tyrosine
-
mutant L105V, pH 7.8, 25°C
5.29
L-tyrosine
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
5.4
L-tyrosine
-
wild-type enzyme, pH 7.8, 25°C
6
L-tyrosine
-
pH 7.5, 25°C, mutant S224A
6.08
L-tyrosine
-
30°C, purified recombinant His-tagged enzyme
6.08
L-tyrosine
-
pH 7.5, 25°C, mutant S226A
6.08
L-tyrosine
-
wild-type enzyme, pH 7.5, 30°C
7.7
L-tyrosine
-
aminoacylation reaction, pH 8.0, wild-type enzyme
11.9
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK
12
L-tyrosine
-
pH 7.6, 37°C, wild-type enzyme
12.3
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 144AcK
12.5
L-tyrosine
recombinant wild-type enzyme, pH 7.8, 25°C
14.2
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant wild-type enzyme
15
L-tyrosine
recombinant truncated mutant enzyme, pH 7.8, 25°C
30
L-tyrosine
-
pH 7.5, 25°C, mutant K231A
31
L-tyrosine
-
pH 7.5, 25°C, mutant S225A
45
L-tyrosine
-
pH 7.5, 25°C, wild-type enzyme
0.046
tRNATyr
-
-
0.15
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 85AcK
0.29
tRNATyr
55°C, pH 8.0
0.29
tRNATyr
wild type enzyme, at 55°C, in 100 mM HEPES-NaOH (pH 8.0), 10 mM MgCl2, 10 mM KCl
1.09
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 355AcK
1.17
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 144AcK
1.32
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant wild-type enzyme
0.07
tRNATyr(G34C)
37°C, pH 7.5, wild-type enzyme
-
0.079
tRNATyr(G34C)
37°C, pH 7.5, mutant enzyme D268R
-
0.12
tRNATyr(wild-type)
37°C, pH 7.5, mutant enzyme D268R
-
0.19
tRNATyr(wild-type)
37°C, pH 7.5, wild-type enzyme
-
additional information
additional information
-
-
additional information
additional information
-
-
-
additional information
additional information
-
mutants
-
additional information
additional information
-
influence of assay conditions, kcat for diverse tRNA variants, overview
-
additional information
additional information
-
the C-terminal His-tag of the recombinant enzyme has little effect on the catalytic activity
-
additional information
additional information
-
kinetic parameters for anticodon mutants of tRNATyr and for for acceptor stem mutants of tRNATyr
-
additional information
additional information
kinetic parameters for anticodon mutants of tRNATyr and for for acceptor stem mutants of tRNATyr
-
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0.1
3-(3,4-dichlorophenyl)-4-(2-(4-methylpiperazin-1-yl)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.1
3-(3,4-difluorophenyl)-4-(2-(piperidin-1-yl)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.1
3-(3,4-dimethoxyphenyl)-4-(2-(4-methylpiperazin-1-yl)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.1
3-(3,4-dimethoxyphenyl)-4-(2-(piperidin-1-yl)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.0243
3-(3-bromophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0205
3-(3-chlorophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0256
3-(3-hydroxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0375
3-(3-methoxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0024
3-(4-bromophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.00062
3-(4-chlorophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0001
3-(4-hydroxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0328
3-(4-methoxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0536
3-phenyl-4-(2-(piperidin-1-yl)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0291
3-phenyl-4-(2-(propylamino)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0355
3-phenyl-4-(2-(pyrrolidin-1-yl)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0165
4-(2-(2,4-dichlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0502
4-(2-(2,4-dihydroxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0052
4-(2-(2,5-dichlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.1
4-(2-(2-(4-nitrophenyl)hydrazinyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.0568
4-(2-(2-chlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0414
4-(2-(2-hydroxyphenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0647
4-(2-(2-methoxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.1
4-(2-(2-methylphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
IC50 above 0.1 mM, in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0182
4-(2-(2-nitrophenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0334
4-(2-(3,4-dichlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0753
4-(2-(3,4-dihydroxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0838
4-(2-(3,4-dimethoxyphenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0067
4-(2-(3,5-dihydroxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0035
4-(2-(3-bromophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0011
4-(2-(3-chlorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.1
4-(2-(3-chlorophenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
IC50 above 0.1 mM, in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0009
4-(2-(3-chlorophenylformyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.081
4-(2-(3-methylphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.1
4-(2-(3-nitrophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
IC50 above 0.1 mM, in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.026
4-(2-(3-pyridylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0043
4-(2-(3-trifluoromethylphenylformyoxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0167
4-(2-(4-bromophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0481
4-(2-(4-bromophenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0093
4-(2-(4-chlorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0088
4-(2-(4-chlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0057
4-(2-(4-fluorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0936
4-(2-(4-fluorophenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0075
4-(2-(4-fluorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0079
4-(2-(4-hydroxyphenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.1
4-(2-(4-hydroxyphenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
IC50 above 0.1 mM, in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0112
4-(2-(4-hydroxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0178
4-(2-(4-methylphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0086
4-(2-(4-methylpiperazin-1-yl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0052
4-(2-(4-nitrophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0168
4-(2-(6-hydroxynaphthalen-2-ylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.1
4-(2-(benzylamino)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.0719
4-(2-(butylamino)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.1
4-(2-(cyclohexylamino)ethoxy)-3-(3,4-dimethoxyphenyl)furan-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.0874
4-(2-(cyclohexylamino)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0177
4-(2-(naphthalen-2-ylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0846
4-(2-butyryloxyethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0478
4-(2-hexanoyloxyethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0062
4-(2-morpholinoethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.041
4-(2-octanoyloxyethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0128
4-(2-phenylacetyloxylethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-bromobenzoate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-chlorobenzoate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-chloropyridine-3-carboxylate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-fluorobenzoate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.0921
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-methoxybenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.08862
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-methylbenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-nitrobenzoate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.01898
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-(3-methylphenyl)propanoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.0111
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-(4-methylphenyl)propanoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.07109
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-aminobenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.08313
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-bromobenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.08613
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-chlorobenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.08214
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-fluorobenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.07211
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-hydroxybenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.069
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-methylbenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.083
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-phenylpropanoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.04894
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-aminobenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.05117
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-bromobenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.05523
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-chlorobenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.06514
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-fluorobenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.04476
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-hydroxybenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.05008
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-methylbenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 6-chloropyridine-3-carboxylate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 6-hydroxypyridine-3-carboxylate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.04332
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl benzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl pyridine-3-carboxylate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl pyridine-4-carboxylate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
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evolution
-
phylogenetic relationship of TyrRS sequences, schematic overview
evolution
analysis of evolutionary conservation of KMSKS motif in tyrosyl-tRNA synthetases, YRSs, two YRSs of Pyrococcus horikoshii and Leishmania major have an overall root mean squared deviation calculated as 3.2 A, although the primary sequences for ATP recognition motifs in Pyrococcus horikoshii and Leishmania major YRSs are identical (KMSKS). The KMSKS loop in YRSs is evolutionarily conserved and mediates inter-molecular interactions between YRS and ATP, Conformational landscape of KMSKS loops in YRSs, overview
evolution
analysis of evolutionary conservation of KMSKS motif in tyrosyl-tRNA synthetases, YRSs, two YRSs of Pyrococcus horikoshii and Leishmania major have an overall root mean squared deviation calculated as 3.2 A, although the primary sequences for ATP recognition motifs in Pyrococcus horikoshii and Leishmania major YRSs are identical (KMSKS). The KMSKS loop in YRSs is evolutionarily conserved and mediates inter-molecular interactions between YRS and ATP, Conformational landscape of KMSKS loops in YRSs, overview
evolution
domain organization of TyrRS from eukaryotes and prokaryotes, overview
evolution
mammalian TyrRS has evolved to be significantly less accurate than its bacterial counterpart. Different evolutionary constraints determine the accuracy of translation quality control in eukaryotes and bacteria. Functional comparisons of mammalian and bacterial tyrosyl-tRNA synthetase reveal key differences at residues responsible for amino acid recognition, highlighting differences in evolutionary constraints for translation quality control, overview
evolution
the enzyme belongs to class I of aminoacyl-tRNA synthetases
evolution
the enzyme belongs to the class I aminoacyl-tRNA synthetase family
evolution
TyrRS belongs to the class I aminoacyl-tRNA synthetases (aaRSs), Evolutionary analysis of SerRS and TyrRS, overview
evolution
TyrRS is a member of class I aminoacyl-tRNA synthetases
evolution
-
the enzyme belongs to class I of aminoacyl-tRNA synthetases
-
evolution
-
analysis of evolutionary conservation of KMSKS motif in tyrosyl-tRNA synthetases, YRSs, two YRSs of Pyrococcus horikoshii and Leishmania major have an overall root mean squared deviation calculated as 3.2 A, although the primary sequences for ATP recognition motifs in Pyrococcus horikoshii and Leishmania major YRSs are identical (KMSKS). The KMSKS loop in YRSs is evolutionarily conserved and mediates inter-molecular interactions between YRS and ATP, Conformational landscape of KMSKS loops in YRSs, overview
-
evolution
-
domain organization of TyrRS from eukaryotes and prokaryotes, overview
-
evolution
-
the enzyme belongs to the class I aminoacyl-tRNA synthetase family
-
malfunction
lysine acetylation can be a possible mechanism for modulating aminoacyl-tRNA synthetases enzyme activities, thus affecting translation. Of recombinantly expressed site-specifically acetylated TyrRS variants, TyrRS-85AcK and -235AcK show dramatic decreases in activity. Variant TyrRS-238AcK has no detectable activity, while variants TyrRS-144AcK and -355AcK have similar activities compared to the wild-type TyrRS. TyrRS-85AcK has a fivefold increase in the KM value for ATP, indicating its role in ATP binding. TyrRS-235AcK has slightly changed KM values for both ATP and tyrosine but a 200fold decrease in catalytic efficiency, suggesting its role in catalysis. K235 and K238 of TyrRS characterized in this study are the two lysine residues in the KMSKS motif. Kinetics for acetylated mutant variants, overview
malfunction
of six mutants tested, two are active towards D-Tyr; one of these has an inverted stereospecificity, with a large preference for D-Tyr, but its activity is low
malfunction
reduced amino acid specificity of mammalian tyrosyl-tRNA synthetase is associated with elevated mistranslation of Tyr codons. Mischarging of tRNATyr with noncognate Phe by tyrosyl-tRNA synthetase is responsible for mistranslation. Steady-state kinetic analyses of CHO cytoplasmic tyrosyl-tRNA synthetase reveals a 25fold lower specificity for Tyr over Phe as compared with previously characterized bacterial enzymes, consistent with the observed increase in translation error rates during tyrosine limitation
physiological function
CYT-18 also promotes self-splicing of group I intron RNAs by stabilizing the functional structure in the conserved core
physiological function
-
although native TyrRS has no known cytokine functions, natural proteolysis of secreted TyrRS releases TyrRSMini, which not only has the same aminoacylation activity as native TyrRS when occuring as a dimer, the monomer is inactive, but TyrRSMini also has strong activity for stimulating migration of polymorphonuclear leukocytes. The migration-stimulating activity is dependent on an ELR tripeptide motif, similar to that in CXC cytokines like IL-8, and also has the familiar bell-shaped concentration dependence seen for CXC cytokines. But TyrRSMini does not induce internalization of CXCR1/2. The TyrRSMini monomer is an agonist, while TyrRSMini dimer is an antagonist of induced PMN cell migration
physiological function
-
tyrosyl-tRNA synthetase functions in group I intron splicing
physiological function
aa-tRNA synthesis is a two-step reaction: activation of an amino acid with ATP to form aminoacyl adenylate, followed by transfer of the aminoacyl moiety to the 3' end of the tRNA. The error rate of this first step of translation is largely dependent on the specificity of the aaRS, that is selection of the correct amino acid and tRNA from the respective cellular pools of predominantly noncognate substrates. aaRSs select their cognate tRNAs by exploiting sequence-specific differences between various tRNAs during binding and aminoacylation. Translation of Tyr codons is highly prone to Phe isincorporation during amino acid limitation inCHOcells. CHO cell TyrRS is error-prone and readily aminoacylates tRNATyr with Phe, cf. EC 6.1.1.20. Steady-state kinetic analyses of CHO cytoplasmic tyrosyl-tRNA synthetase reveals a 25fold lower specificity for Tyr over Phe as compared with previously characterized bacterial enzymes, consistent with the observed increase in translation error rates during tyrosine limitation
physiological function
aminoacyl-tRNA synthetases (aaRSs) are housekeeping enzymes essential for protein synthesis. Apart from their parent aminoacylation activity, several aaRSs perform non-canonical functions in diverse biological processes. Leishmania tyrosyl-tRNA synthetase (LdTyrRS) performs aminoacylation and acts as a mimic of host CXC chemokine. Non-canonical function of Leishmania donovani tyrosyl-tRNA synthetase. The enzyme is essential. The released, extracellular LdTyrRS functions as a neutrophil chemoattractant. LdTyrRS specifically binds to host macrophages with its ELR (Glu-Leu-Arg) peptide motif. The ELR-CXCR2 receptor interaction mediates this binding. This interaction triggers enhanced secretion of the proinflammatory cytokines TNF-alpha and interleukin-6 by host macrophages. Possible immunomodulating role of LdTyrRS in Leishmania infection. Triggering of cytokine secretion by LdTyrRS, overview
physiological function
aminoacyl-tRNA synthetases (aaRSs) for glycine, alanine, serine and tyrosine play important roles in fibroin synthesis
physiological function
the flexibility and rapid dynamics of the wild-type aminoacyl-tRNA synthetase catalytic loop structure are crucial for formation of protein-substrate interactions and subsequently for overall enzyme functional activity, dynamic properties of the enzyme, overview
physiological function
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the human TyrRS can be split into two fragments with distinct signaling activities. The N-terminal fragment is an IL-8-like cytokine whereas the C-terminal fragment is more similar to endothelial monocyte-activating polypeptide II (EMAP II). Therapeutic effect of recombinant human tyrosyl-tRNA synthetase (rhTyrRS) against development of thrombocytopenia in cyclophosphamide (CTX) treated mice. Recombinant hTyrRS promotes migration and aggregation of megakaryocytes to the bone marrow niche. 1 is particularly important for the adhesion. The N-terminal fragment of the recombinant TyrRS acts as a chemoattractant molecule for M-07e cells, it stimulates adhesion of THP-1 cells to HUVECs and plays a role in the transendothelial migration of megakaryocytes and thrombocytopoiesis. All mice pretreated with rhTyrRS show a dose-dependent increase in megakaryocytes localized to the sinusoids. Recombinant human TyrRS enhances survival of cyclophosphamide (CTX) treated mice, that the bone marrow endothelial cells may enhance survival of megakaryocytes in the presence of rhTyrRS pretreatment
physiological function
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tyrosyl-tRNA synthetase is a potential kyotorphin synthetase (i.e. tyrosine-arginine ligase, EC 6.3.2.24) in mammals
physiological function
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the flexibility and rapid dynamics of the wild-type aminoacyl-tRNA synthetase catalytic loop structure are crucial for formation of protein-substrate interactions and subsequently for overall enzyme functional activity, dynamic properties of the enzyme, overview
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physiological function
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aminoacyl-tRNA synthetases (aaRSs) are housekeeping enzymes essential for protein synthesis. Apart from their parent aminoacylation activity, several aaRSs perform non-canonical functions in diverse biological processes. Leishmania tyrosyl-tRNA synthetase (LdTyrRS) performs aminoacylation and acts as a mimic of host CXC chemokine. Non-canonical function of Leishmania donovani tyrosyl-tRNA synthetase. The enzyme is essential. The released, extracellular LdTyrRS functions as a neutrophil chemoattractant. LdTyrRS specifically binds to host macrophages with its ELR (Glu-Leu-Arg) peptide motif. The ELR-CXCR2 receptor interaction mediates this binding. This interaction triggers enhanced secretion of the proinflammatory cytokines TNF-alpha and interleukin-6 by host macrophages. Possible immunomodulating role of LdTyrRS in Leishmania infection. Triggering of cytokine secretion by LdTyrRS, overview
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additional information
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dissociating quaternary structures regulating novel functions of other tRNA synthetases
additional information
enzyme MtTyrRS contains the HIGH-like and KFGKS catalytic motifs that catalyze amino acid activation with ATP.The conformational mobility of MtTyrRS catalytic KFGKS loop is analyzed by 100-ns all-atoms molecular dynamics simulations of the free enzyme and its complexes with different substrates: tyrosine, ATP, and the tyrosyl-adenylate intermediate. In the closed state of the active site, the KFGKS loop, readily adopts different stable conformations depending on the type of bound substrate. The closed state of the loop is stabilized by dynamic formation of two antiparallel beta-sheets at flanking ends which hold the KFGKS fragment inside the active center. Molecular dynamics simulations, conformation of the MtTyrRS catalytic loop in substrate?bound states, detailed overview
additional information
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enzyme MtTyrRS contains the HIGH-like and KFGKS catalytic motifs that catalyze amino acid activation with ATP.The conformational mobility of MtTyrRS catalytic KFGKS loop is analyzed by 100-ns all-atoms molecular dynamics simulations of the free enzyme and its complexes with different substrates: tyrosine, ATP, and the tyrosyl-adenylate intermediate. In the closed state of the active site, the KFGKS loop, readily adopts different stable conformations depending on the type of bound substrate. The closed state of the loop is stabilized by dynamic formation of two antiparallel beta-sheets at flanking ends which hold the KFGKS fragment inside the active center. Molecular dynamics simulations, conformation of the MtTyrRS catalytic loop in substrate?bound states, detailed overview
additional information
lysine acetylation could be a possible mechanism for modulating aminoacyl-tRNA synthetases enzyme activities, thus affecting translation
additional information
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lysine acetylation could be a possible mechanism for modulating aminoacyl-tRNA synthetases enzyme activities, thus affecting translation
additional information
molecular dynamics modeling of substrates L- and D-Tyr into the active site of wild-type enzyme and mutants D81R and E36Q using the PDB ID 1J1U X-ray structure, superimposed based on their protein/tRNA environment, enzyme molecular dynamics simulation amd modeling, structure-function analysis, detailed overview
additional information
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molecular dynamics modeling of substrates L- and D-Tyr into the active site of wild-type enzyme and mutants D81R and E36Q using the PDB ID 1J1U X-ray structure, superimposed based on their protein/tRNA environment, enzyme molecular dynamics simulation amd modeling, structure-function analysis, detailed overview
additional information
residues, not conserved between bacteria and eukaryotes, Cys35, His48, Thr51, and Lys233 in bacterial TyrRS interact with ATP during transition state formation. Comparison the Geobacillus stearothermophilus, PDB ID 1tyd, and human, PDB ID 1q11, TyrRS active sites, overview. Hydrogen-bonding interactions between bacterial TyrRS residues Asp176 and Tyr34 and the substrate Tyr hydroxyl group help confer amino acid specificity to the enzyme
additional information
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residues, not conserved between bacteria and eukaryotes, Cys35, His48, Thr51, and Lys233 in bacterial TyrRS interact with ATP during transition state formation. Comparison the Geobacillus stearothermophilus, PDB ID 1tyd, and human, PDB ID 1q11, TyrRS active sites, overview. Hydrogen-bonding interactions between bacterial TyrRS residues Asp176 and Tyr34 and the substrate Tyr hydroxyl group help confer amino acid specificity to the enzyme
additional information
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the LdTyrRS polypeptide chain consists of two pseudo-monomers, each consisting of two domains. Comparing the two independent chains in the asymmetric unit reveals that the two pseudo-monomers of LdTyrRS can bend with respect to each other essentially as rigid bodies. This flexibility might be useful in the positioning of tRNA for catalysis since both pseudo-monomers in the LdTyrRS chain are needed for charging tRNATyr. The LdTyrRS active site contains two critical pockets: the tyrosine binding pocket (YBP) where the tyrosyl group of inhibitor TyrSA is situated, and the adenine binding pocket (ABP) where the adenine moiety of TyrSA binds. Residues making hydrogen bonds with the TyrSA tyrosyl group in the tyrosine binding pocket (YBP) are Y36, Y163, Q167, D170 and Q185. Residues G38, A72 and F75 are responsible for the hydrophobic interactions between enzyme and tyrosine moiety in the YBP. An extra pocket (EP) appears to be present near the adenine binding. The extra pocket appears to be present near the adenine binding region of LdTyrRS, this pocket is absent in the two human homologous enzymes. Structure-based modelling, overview
additional information
the TyrRS stereospecificity is robust towards charge rearrangements near the ligand. Whereas most aminoacyl-tRNA synthetases (aaRSs) have a strong preference for their L-amino acid substrate, TyrRS has a detectable, natural activity for the D-tyrosine stereoisomer, only tenfold less than for L-Tyr; additional protection against D-Tyr is usually provided by another enzyme, D-aminoacyl-tRNA hydrolase. Enzyme molecular dynamics simulations using the crystal structure of Escherichia coli TyrRS bound to a tyrosyl adenylate analogue, PDB ID 1VBM
additional information
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the TyrRS stereospecificity is robust towards charge rearrangements near the ligand. Whereas most aminoacyl-tRNA synthetases (aaRSs) have a strong preference for their L-amino acid substrate, TyrRS has a detectable, natural activity for the D-tyrosine stereoisomer, only tenfold less than for L-Tyr; additional protection against D-Tyr is usually provided by another enzyme, D-aminoacyl-tRNA hydrolase. Enzyme molecular dynamics simulations using the crystal structure of Escherichia coli TyrRS bound to a tyrosyl adenylate analogue, PDB ID 1VBM
additional information
tyrosyl-tRNA synthetase structure comparisons, the KMSKS loop is very variable in conformation, intrinsic conformational heterogeneity in KMSKS loop that is independent of occupancy of active site. Differential centroid distance analyses between KMSKS motif and Rossmann fold domain reveal an intriguing bimodal distribution. The KMSKS loop is positioned at the intersection of Rossmann fold and the C-terminal region and plays a role in ATP binding and catalysis. KMSKS loop orientation and conformation can be independent of ATP binding, conformational flexibility of KMSKS loop, overview
additional information
tyrosyl-tRNA synthetase structure comparisons, the KMSKS loop uís very variable in conformation, intrinsic conformational heterogeneity in KMSKS loop that is independent of occupancy of active site. Differential centroid distance analyses between KMSKS motif and Rossmann fold domain reveal an intriguing bimodal distribution. The KMSKS loop is positioned at the intersection of Rossmann fold and the C-terminal region and plays a role in ATP binding and catalysis. KMSKS loop orientation and conformation can be independent of ATP binding, conformational flexibility of KMSKS loop, overview
additional information
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enzyme MtTyrRS contains the HIGH-like and KFGKS catalytic motifs that catalyze amino acid activation with ATP.The conformational mobility of MtTyrRS catalytic KFGKS loop is analyzed by 100-ns all-atoms molecular dynamics simulations of the free enzyme and its complexes with different substrates: tyrosine, ATP, and the tyrosyl-adenylate intermediate. In the closed state of the active site, the KFGKS loop, readily adopts different stable conformations depending on the type of bound substrate. The closed state of the loop is stabilized by dynamic formation of two antiparallel beta-sheets at flanking ends which hold the KFGKS fragment inside the active center. Molecular dynamics simulations, conformation of the MtTyrRS catalytic loop in substrate?bound states, detailed overview
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additional information
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tyrosyl-tRNA synthetase structure comparisons, the KMSKS loop is very variable in conformation, intrinsic conformational heterogeneity in KMSKS loop that is independent of occupancy of active site. Differential centroid distance analyses between KMSKS motif and Rossmann fold domain reveal an intriguing bimodal distribution. The KMSKS loop is positioned at the intersection of Rossmann fold and the C-terminal region and plays a role in ATP binding and catalysis. KMSKS loop orientation and conformation can be independent of ATP binding, conformational flexibility of KMSKS loop, overview
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additional information
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molecular dynamics modeling of substrates L- and D-Tyr into the active site of wild-type enzyme and mutants D81R and E36Q using the PDB ID 1J1U X-ray structure, superimposed based on their protein/tRNA environment, enzyme molecular dynamics simulation amd modeling, structure-function analysis, detailed overview
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purified selenomethionyl-TyrRSapm in complex with tyrosinol, crystallization is improved by introducing anion-exchange chromatography, vapour diffusion method, 0.002 ml of 14 mg/ml protein in 20 mM Tris-HCl, pH 7.4, 25°C, is mixed with 500 nl reservoir solution containing 0.1 M sodium citrate, pH 5.5, and 6-9% PEG 4000 w/v, 15% 2-methyl-2,4-pentane-d12-diol, 0.1 M KCl, 1 mM MgCl2, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement
crystal of SeMet-substituted TyrRS is obtained by the microbatch method, using an automatic crystallization robot. The crystals are grown at 20°C in a month. The crystal of native TyrRS is obtained by hanging-drop, vapor-diffusion method. Crystals of SeMet-substituted TyrRS belong to the space group P4(3)2(1)2, with unit cell parameters a = b = 66.66 A, c = 197.48 A. Crystals of native TyrRS belong to the space group P4(3)2(1)2 with unit cell parameters a = b = 65.91 A, c = 196.17 A
hanging-drop vapour-diffusion method, The crystals belong to the tetragonal space group P4(3)2(1)2, with unit-cell parameters a = b = 66.1, c= 196.2 A, and diffract to beyond 2.15 A resolution
hanging-drop, vapor-diffusion method. Crystals belong to the space group P2(1), with unit cell parameters a = 40.62 A, b = 96.16 A, c = 92.64 A, beta = 94.41°
hanging drop vapor-diffusion method. Crystal structures of TyrRS catalytic domain, in complex with L-tyrosine and L-tyrosyladenylate analogue, 5'-O-[N-(L-tyrosyl)sulfamoyl]adenosine, are solved at 2.0 A and 2.7 A resolution
the iodoTyrRS-ec-3-azide-L-tyrosine structure is determined at a resolution of 1.8 A
electron density map, X-ray structure
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T51 mutants of tyrosyl-tRNA synthetase
X-ray diffraction, at 2.7 A resolution, structure analysis of the enzyme-ligand complex, e.g. with specific synthetic inhibitors, molecular modeling
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mutant mt-TyrRS-DS4, lacking the C-terminal S4-like domain, in complex with Tyr-AMS, an adenylate analogue, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement
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purified tyrosyl-tRNA synthetase in complex with a nanobody and inhibitory tyrosyl adenylate analogue TyrSA, purified LdTyrRS and NbA proteins are incubated on ice for 30 min at a 1:2 M ratio followed by buffer exchange to crystallization buffer. The protein complex is then incubated with 0.2 mM of TyrSA (5'-O-[N-(L-tyrosyl)sulfamoyl]adenosine) on ice for 30-60 min, sitting drop vapour diffsuion method, mixing of 0.001 ml of protein solution containing 5 mg/ml protein complex in 25 mM HEPES, pH 7.25, 100 mM NaCl, 1 mM TCEPHCl, 5% glycerol, and 0.025% NaN3, with 0.001 ml of reservoir solution containing 0.1 M sodium cacodylate, pH 5.7, and 22% PEG 4000, room temperature, 5-7 days, X-ray diffraction structure determination and analysis at 2.75 A resolution, modeling
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purified recombinant C-terminally His6-tagged tyrosyl aminoacyl-tRNA synthetase, sitting-drop vapor diffusion technique, 15 mg/ml protein in 20 mM Tris, pH 8.5, 50 mM NaCl, 10 mM 2-mercaptoethanol, crystals are grown either in the presence of 2 mM 4-bromophenylalanine or 3-(2-naphthyl)alanine at 20°C or 4°C, against a mother liquor composed of 16-20% PEG 300, 3-5% PEG 8000, 100 mM Tris, pH 8.8-pH 8.2, and 10% glycerol by mixing of equla volumes, X-ray diffraction structure determination and analysis at 1.9 A resolution
sitting-drop vapor-diffusion method. Space group P2(1)2(1)2(1) with two molecules per asymmetric unit, with unit cell dimensions a = 45.12 A, b = 185.29 A, and c = 95.48 A. Crystal structures for the apo wild-type and O-methyl-L-tyrosine-specific mutant enzyme are determined at 2.66 A and 3.0 A
structure of the TyrRS-tRNA(Tyr)-L-tyrosine complex, solved at a resolution of 1.95 A
hanging-drop vapour diffusion method. The crystals belong to the monoclinic space group P2(1) with unit-cell parameters a = 49.2 A, b = 156.5 A, c = 55.2 A, beta = 94.2
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1.95 A crystal structure of mutant DELTA424-669 of CYT-18 protein. DELTA424-669 crystals are grown by sitting-drop vapor diffusion. The crystals are in space group C2 with unit cell dimensions: a = 104.88 A, b = 73.21 A, c = 56.79 A, beta = 111.35°
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a 4.5 A co-crystal structure of the Twort orf 142-I2 group I intron ribozyme bound to splicing-active, carboxy-terminally truncated CYT-18. Structure shows that the group I intron binds across the two subunits of the homodimeric protein with a newly evolved RNA-binding surface distinct from that which binds tRNATyr. This RNA binding surface provides an extended scaffold for the phosphodiester backbone of the conserved catalytic core of the intron RNA, allowing the protein to promote the splicing of a wide variety of group I introns. The group I intron-binding surface includes three small insertions and additional structural adaptations relative to non-splicing bacterial TyrRSs, indicating a multistep adaptation for splicing function
hanging-drop, vapor-diffusion method. Crystals belong to the space group P2(1)2(1)2(1), with unit cell parameters a = 74.35 A, b = 88.26 A, c = 162.92 A
crystal structure at 2.3 A resolution
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purified recombinant modified enzyme, SceTyrRS comprising residues 1-364, as ternary complex with cognate tRNATyr and Tyr-AMP analog O-(adenosine-5'-O-yl) N-(L-tyrosyl)phosphoramidate, i.e. Tyr-AMPN, hanging-drop vapor diffusion method, mixing of equal volumes of protein solution containing ca. 0.2 mM SceTyrRS, 5 mM Tyr-AMPN, ca. 0.2 mM tRNATyr, 40 mM KCl in 20 mM Tris buffer at pH 7.5, with reservoir solution containing 25% v/v PEG 400 and 100 mM CaCl2 in 100 mM Tris buffer at pH 7.5, X-ray diffraction structure determination and analysis at 2.4 A resolution
crystal structure determination by X-ray diffraction, enzyme complexed with inhibitors at 2.8 A resolution, and truncated enzyme complexed with inhibitors at 2.2 A resolution
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enzyme complexed to a tyrosyl aryl dipeptide inhibitor, structure analysis
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pure enzyme, 12 mg/ml, or in complex with tyrosinol, hanging drop vapour diffusion technique, equal volumes of protein and a reservoir solution that contains 1.2 M ammonium sulfate, 10 mM MgCl2, 0.5 mM dithiothreitol, 50 mM MES, pH 5.8, X-ray diffraction structure determination and analysis, enzyme in complex with tyrosinol, ATP and tRNATyr, at 293K, equilibration of 0.004 ml protein-RNA solution against 1 ml reservoir solution, protein-RNA solution: 4-5 mg/ml of enzyme in a molar ratio of 1:1 or 1:2 with RNA, 5 mM tyrosinol, 10 mg MgCl2, 10 mM ATP, 50 mM HEPES, pH 7.0, 0.8 M ammonium sulfate, reservoir solution: 1.5-1.6 M ammonium sulfate, 0.1 M HEPES, pH 7.0, 2-4 weeks, X-ray diffraction structure determination at 2.0-2.1 A resolution and analysis
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H306A
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no complementation of the thermosensitive Escherichia coli tyrS mutant HB2109, 3fold decrease in kcat for amino acid activation
H306D
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no complementation of the thermosensitive Escherichia coli tyrS mutant HB2109
H53A
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no complementation of the thermosensitive Escherichia coli tyrS mutant HB2109, inactive
K395N
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slight complementation of the thermosensitive Escherichia coli tyrS mutant HB2109, 17fold increase in Km for Escherichia coli tRNATyr, reduced activity
S356A
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no complementation of the thermosensitive Escherichia coli tyrS mutant HB2109, 7fold increase in Km for Escherichia coli tRNATyr, reduced activity
D172H
mutant enzyme shows a significant reductions in tyrosylation activity
D172N
mutant enzyme shows a significant reductions in tyrosylation activity
Y39E
mutant enzyme maintains tyrosylation activity
Y39K
mutant enzyme maintains tyrosylation activity
D172H
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mutant enzyme shows a significant reductions in tyrosylation activity
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D172N
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mutant enzyme shows a significant reductions in tyrosylation activity
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Y39G
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mutant enzyme maintains tyrosylation activity. Although the wild-type enzyme shows specific tyrosylation activity but not aminoacylation activity for 4-azido-L-phenylalanine, the Y39G mutant exhibits near identical aminoacylation activity of both tyrosine and 4-azido-L-phenylalanine
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Y39G/D172P
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reduction in tyrosylation activity, the mutant shows specific aminoacylation activity for 4-azide-L-phenylalanine
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E91N
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mutation of the ELR motif: mutant protein does not induce phosphorylation of VEGFR2, suggesting that the ELR motif in mini-TyrRS has an important role in transactivation of VEGFR2
L92Y
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mutation of the ELR motif: mutant protein does not induce phosphorylation of VEGFR2, suggesting that the ELR motif in mini-TyrRS has an important role in transactivation of VEGFR2
R93Q
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mutation of the ELR motif: mutant protein does not induce phosphorylation of VEGFR2, suggesting that the ELR motif in mini-TyrRS has an important role in transactivation of VEGFR2
A74G
site-directed mutagenesis, replacement of Ala74 with Gly increases the Km 7fold and has no effect on kcat for Tyr. The kcat/Km for Phe decreases 5fold
D122N
site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme
G120N
site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme
H77T
site-directed mutagenesis, mutation of His77 to the smaller nonhydrophobic Thr increases the Km and decreases the kcat by 40fold
L125W
site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme
N82D
site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme
W40C
site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme
Y123W
site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme
Y52H
site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme
D41N
site-directed mutagenesis
D81H/Q179E/Q201D
site-directed mutagenesis, the mutant shows no activity for L-Tyr and D-Tyr
D81K/Q179E
site-directed mutagenesis, the mutant shows no activity for L-Tyr and D-Tyr
D81K/Q179E/Q201D
site-directed mutagenesis, the mutant shows no activity for L-Tyr and D-Tyr
D81N
site-directed mutagenesis, the mutant shows a preference for L-Tyr that is much stronger than for the wild-type TyrRS. The ligand ammonium is coordinated at the L-Tyr endpoint by Asp41 (which replaces Asp81 in the coordination shell) and Tyr175 but not Gln179. At the D-Tyr endpoint, the ligand ammonium is coordinated by a mixture of Gln201, Tyr175, Asp41, and sometimes weakly by Gln179
D81R
site-drected mutagenesis, the mutant shows low activity for L-Tyr and D-Tyr, and the same KM value for L-Tyr compared to wild-type enzyme, the mutant is D-Tyr specific, but with low activity
F130S
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construction of a plasmid library of randomly mutated gene tyrS by PCR, isolation of a mutant R-6-A-7 which incorporates L-beta-(5-hydroxy-2-pyridyl)-alanine in transformed Escherichia coli cells in vivo, increased temperature instability
Q179A
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site-directed mutagenesis, reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q179N
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site-directed mutagenesis, reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q179S
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site-directed mutagenesis, reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195A
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site-directed mutagenesis, active with L-tyrosine, low activity with 3-iodo-L-tyrosine
Q195C
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site-directed mutagenesis, reduced activity with L-tyrosine, low activity with 3-iodo-L-tyrosine
Q195D
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site-directed mutagenesis, highly reduced activity with L-tyrosine, low activity with 3-iodo-L-tyrosine
Q195E
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site-directed mutagenesis, active with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195G
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site-directed mutagenesis, reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195H
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site-directed mutagenesis, active with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195I
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site-directed mutagenesis, highly reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195L
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site-directed mutagenesis, reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195M
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site-directed mutagenesis, highly reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195N
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site-directed mutagenesis, reduced activity with L-tyrosine, low activity with 3-iodo-L-tyrosine
Q195S
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site-directed mutagenesis, active with L-tyrosine, low activity with 3-iodo-L-tyrosine
Q195T
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site-directed mutagenesis, active with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195V
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site-directed mutagenesis, reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195Y
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site-directed mutagenesis, reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Y37A/Q195A
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inactive mutant
Y37A/Q195C
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site-directed mutagenesis, active with L-tyrosine and 3-iodo-L-tyrosine, preference for the latter, reduced overall activity
Y37A/Q195N
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inactive mutant
Y37A/Q195S
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site-directed mutagenesis, equally low activity with L-tyrosine and 3-iodo-L-tyrosine
Y37I/Q195A
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site-directed mutagenesis, equally low activity with L-tyrosine and 3-iodo-L-tyrosine
Y37I/Q195C
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inactive mutant
Y37I/Q195N
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inactive mutant
Y37I/Q195S
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inactive mutant
Y37L/Q195A
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site-directed mutagenesis, highly reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Y37L/Q195C
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site-directed mutagenesis, equally low activity with L-tyrosine and 3-iodo-L-tyrosine
Y37L/Q195N
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site-directed mutagenesis, highly reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Y37L/Q195S
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inactive mutant
Y37V/Q195N
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site-directed mutagenesis, active with L-tyrosine and 3-iodo-L-tyrosine, preference for the latter, reduced overall activity
Y37V/Q195S
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site-directed mutagenesis, reduced activity with L-tyrosine and 3-iodo-L-tyrosine
Y73A
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site-directed mutagenesis, equally active with L-tyrosine and 3-iodo-L-tyrosine
Y73F
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site-directed mutagenesis, active with L-tyrosine, no activity with 3-iodo-L-tyrosine
Y73G
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site-directed mutagenesis, equally active with L-tyrosine and 3-iodo-L-tyrosine, reduced overall activity
Y73H
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site-directed mutagenesis, active with L-tyrosine, and slightly active with 3-iodo-L-tyrosine
Y73I
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site-directed mutagenesis, active with L-tyrosine and 3-iodo-L-tyrosine, preference for the latter
Y73L
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site-directed mutagenesis, equally active with L-tyrosine and 3-iodo-L-tyrosine
Y73M
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site-directed mutagenesis, equally active with L-tyrosine and 3-iodo-L-tyrosine
Y73S
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site-directed mutagenesis, active with L-tyrosine and 3-iodo-L-tyrosine, preference for the first
Y73V
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site-directed mutagenesis, equally active with L-tyrosine and 3-iodo-L-tyrosine
Y73V/Q195A
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site-directed mutagenesis, active with L-tyrosine and 3-iodo-L-tyrosine, preference for the latter, reduced overall activity
Y73V/Q195C
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site-directed mutagenesis, 10fold more active with 3-iodo-L-tyrosine than with L-tyrosine, reduced overall activity
C35G
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crystal structure of mutants Cys to Gly35 and Tyr to Phe34
D194A
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site-directed mutagenesis, mutation does not affect the initial binding of the tRNATyr substrate, it does not destabilize the transition state complex for the second reaction step
D78A
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site-directed mutagenesis, mutation does not affect the initial binding of the tRNATyr substrate, it does not destabilize the transition state complex for the second reaction step
I52L
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unaltered enzyme activity in the diphosphate exchange reaction, decreased kinetic stability at 68.5°C compared to the wild-type, compensates mutation L105V partially, destabilized association between subunits
K233A
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mutant shows a reduced affinity for ATP
L105V
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unaltered enzyme activity in the diphosphate exchange reaction, decreased kinetic stability at 68.5°C compared to the wild-type, destabilization of the monomeric intermediate of unfolding, mutation can be partially compensated by mutation I52L
M55L
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increase in kinetic stability at 68.5°C compared to the wild-type, mutation is not coupled to others in its effects, slightly increased kinetic stability at 68.5°C
Q173A
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site-directed mutagenesis, mutation does not affect the initial binding of the tRNATyr substrate, it destabilizes the transition state complex for the second reaction step
Q195A
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site-directed mutagenesis, mutation does not affect the initial binding of the tRNATyr substrate, it does not destabilize the transition state complex for the second reaction step
T234A
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decrease of the forward rate constant by 540fold, 3fold increase in affinity of the enzyme for ATP
T34F
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crystal structure of mutants Cys to Gly35 and Tyr to Phe34
T51A
the mutant demonstrates an increase in activity
T51G
the mutant demonstrates an increase in activity
T51S
the mutant demonstrates an increase in activity
Y169A
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site-directed mutagenesis, mutation does not affect the initial binding of the tRNATyr substrate, it does not destabilize the transition state complex for the second reaction step
E196K
-
naturally occuring mutation in the autosomal dominant intermediate Charcot-Marie-Tooth neuropathy type C disorder, the mutant enzyme shows reduced activity and specific distribution in the cell compared to the wild-type enzyme, no functional complementation of a Saccharomyces cerevisiae TYS1 mutant strain, the mutant shows altered distribution in neuronal cells compared to the wild-type enzyme when recombinantly expressed
G41R
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naturally occuring mutation in the autosomal dominant intermediate Charcot-Marie-Tooth neuropathy type C disorder, the mutant enzyme shows reduced activity and specific distribution in the cell compared to the wild-type enzyme, partial functional complementation of a Saccharomyces cerevisiae TYS1 mutant strain, the mutant shows altered distribution in neuronal cells compared to the wild-type enzyme when recombinantly expressed
K231A
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site-directed mutagenesis, no effect on the catalytic activity of the enzyme
M252A
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site-directed mutagenesis, the mutant is fully active in ATP/diphosphate exchange, indicating that the site for tyrosyl-adenylate formation remains unperturbed upon mutation, tRNA mutant U73 is no more charged by mt-TyrRS upon Met252Ala mutation, the weak tyrosylation activity of tRNATyr with G73 is completely abolished, mutating Met252 shows only faint effects on wild-type and mutants mt-tRNATyr charging as compared to the wild-type enzyme
mini-TyrRS_D173A
binding pocket variant, retains cytokine function
mini-TyrRS_TyrRS(ELQ)
the surface helix encodes an ELR motif that functions like the ELR tripeptide in CXC cytokines, substitution of Arg93 to generate ELQ
mini-TyrRS_TyrRS(EYR)
the surface helix encodes an ELR motif that functions like the ELR tripeptide in CXC cytokines, substitution of Leu92 to generate EYR
mini-TyrRS_TyrRS(NLR)
the surface helix encodes an ELR motif that functions like the ELR tripeptide in CXC cytokines, substitution of Glu91 to generate NLR
mini-TyrRS_Y39A
binding pocket variant, retains cytokine function
mini-TyrRS_Y39A/D173A
binding pocket variant, retains cytokine function
Q202A
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site-directed mutagenesis, the mutant is fully active in ATP/diphosphate exchange, indicating that the site for tyrosyl-adenylate formation remains unperturbed upon mutation, the weak tyrosylation activity of tRNATyr with G73 is completely abolished, mutating Gln202 shows only faint effects on wild-type and mutants mt-tRNATyr charging as compared to the wild-type enzyme
S200A
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site-directed mutagenesis, the mutant is fully active in ATP/diphosphate exchange, indicating that the site for tyrosyl-adenylate formation remains unperturbed upon mutation, replacing Ser200 with Glu completely abolishes tyrosylation activity of wild-type and mutated tRNATyr transcripts
S224A
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site-directed mutagenesis, 7.5fold decrease of the forward rate constant
S225A
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site-directed mutagenesis, no effect on the catalytic activity of the enzyme
S226A
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site-directed mutagenesis, 60fold decrease of the forward rate constant
TyrRS_153-156delVKQV
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dominant-intermediate Charcot-Marie-Tooth neuropathy associated mutation
TyrRS_E196K
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dominant-intermediate Charcot-Marie-Tooth neuropathy associated mutation
TyrRS_G41R
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dominant-intermediate Charcot-Marie-Tooth neuropathy associated mutation
AMSSS
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TyrRS mutant, a library of more than 200 mutants substituting the ATP binding motif KMSSS is built
D286R
the mutant enzyme aminoacylates the amber suppressor tRNA, as well as the wild-type tRNATyr, whereas the wild-type enzyme aminoacylates the amber suppresssor tRNA about 300fold less efficientyl than the wild-type tRNATyr. The mutant recognizes the amber suppressor tRNA 65fold better than the wild-type enzyme. The activity if the mutant and amber suppressor tRNA pair is as high as 22% that of the wild-type pair. The mutation mainly decreases the KM for tRNA. The kcat is not affected as much
D81R
site-diretced mutagenesis, the mutant shows reduced stereospecificity for L-Tyr compared to wild-type
E36Q
site-diretced mutagenesis, the mutant shows increased, but not inverted, stereospecificity for L-Tyr compared to wild-type
KMGCA
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TyrRS mutant, a library of more than 200 mutants substituting the ATP binding motif KMSSS is built
RMSSS
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TyrRS mutant, a library of more than 200 mutants substituting the ATP binding motif KMSSS is built
Y32Q/D158A
site-directed mutagenesis, enzyme mutant discriminates between L-tyrosine and O-methyl-L-tyrosine, with a high activity only with the latter
Y32Q/D158A/L162P/D286R
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The engineered enzyme is improved with specificity for O-methyl-L-tyrosine and 10fold improved incorporation. The optimized synthetase is used for the preparative expression of a modified uvGFP carrying MeTyr at position 66 as part of its fluorophore. This biosynthetic protein shows quantitative incorporation of the non-natural amino acid, The Asp286Arg mutation serves for improved recognition of the CUA anticodon
D286R
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the mutant enzyme aminoacylates the amber suppressor tRNA, as well as the wild-type tRNATyr, whereas the wild-type enzyme aminoacylates the amber suppresssor tRNA about 300fold less efficientyl than the wild-type tRNATyr. The mutant recognizes the amber suppressor tRNA 65fold better than the wild-type enzyme. The activity if the mutant and amber suppressor tRNA pair is as high as 22% that of the wild-type pair. The mutation mainly decreases the KM for tRNA. The kcat is not affected as much
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D81R
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site-diretced mutagenesis, the mutant shows reduced stereospecificity for L-Tyr compared to wild-type
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E36Q
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site-diretced mutagenesis, the mutant shows increased, but not inverted, stereospecificity for L-Tyr compared to wild-type
-
Y43G
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broadened amino acid substrate specificity
YARS_153-156delVKQV
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dominant-intermediate Charcot-Marie-Tooth neuropathy associated mutation
YARS_E196K
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dominant-intermediate Charcot-Marie-Tooth neuropathy associated mutation
YARS_G41R
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dominant-intermediate Charcot-Marie-Tooth neuropathy associated mutation
D172P
mutant enzyme shows a significant reductions in tyrosylation activity
D172P
the mutation completely abolishes tyrosylation activity
Y39G
mutant enzyme maintains tyrosylation activity. Although the wild-type enzyme shows specific tyrosylation activity but not aminoacylation activity for 4-azido-L-phenylalanine, the Y39G mutant exhibits near identical aminoacylation activity of both tyrosine and 4-azido-L-phenylalanine
Y39G
the mutant exhibits near identical aminoacylation activity of both L-tyrosine and 4-azide-L-phenylalanine
Y39G/D172P
reduction in tyrosylation activity, the mutant shows specific aminoacylation activity for 4-azide-L-phenylalanine
Y39G/D172P
the double mutant shows a reduction in tyrosylation activity
T51P
-
increased enzyme activity in the diphosphate exchange reaction, decreased kinetic stability at 68.5°C compared to the wild-type, slightly destalized mutant
T51P
the mutant demonstrates a 25fold increase in activity compared to the wild type enzyme
additional information
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Asp172 mutants shows completely abolished tyrosylation activity, whereas mutation at Tyr39 has no effect on activity
additional information
Asp172 mutants shows completely abolished tyrosylation activity, whereas mutation at Tyr39 has no effect on activity
additional information
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Asp172 mutants shows completely abolished tyrosylation activity, whereas mutation at Tyr39 has no effect on activity
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additional information
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interaction analysis of deletion and truncation mutants, overview
additional information
generation of a truncated mutant enzyme TyrRS
additional information
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generation of a truncated mutant enzyme TyrRS
additional information
computational mutant design using the crystal structure of Escherichia coli TyrRS bound to a tyrosyl adenylate analogue, PDB ID 1VBM
additional information
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computational mutant design using the crystal structure of Escherichia coli TyrRS bound to a tyrosyl adenylate analogue, PDB ID 1VBM
additional information
of recombinantly expressed site-specifically acetylated TyrRS variants, TyrRS-85AcK and -235AcK show dramatic decreases in activity. Variant TyrRS-238AcK has no detectable activity, while variants TyrRS-144AcK and -355AcK have similar activities compared to the wild-type TyrRS. TyrRS-85AcK has a fivefold increase in the KM value for ATP, indicating its role in ATP binding. TyrRS-235AcK has slightly changed KM values for both ATP and tyrosine but a 200fold decrease in catalytic efficiency, suggesting its role in catalysis
additional information
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of recombinantly expressed site-specifically acetylated TyrRS variants, TyrRS-85AcK and -235AcK show dramatic decreases in activity. Variant TyrRS-238AcK has no detectable activity, while variants TyrRS-144AcK and -355AcK have similar activities compared to the wild-type TyrRS. TyrRS-85AcK has a fivefold increase in the KM value for ATP, indicating its role in ATP binding. TyrRS-235AcK has slightly changed KM values for both ATP and tyrosine but a 200fold decrease in catalytic efficiency, suggesting its role in catalysis
additional information
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altered specificity for amino acid
additional information
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kinetic properties ATP-diphosphate exchange reacion of engineered mutants
additional information
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effects of coupling of mutations on thermal stability
additional information
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disrupted function and axonal distribution of the mutant enzyme in autosomal dominant intermediate Charcot-Marie-Tooth neuropathy type C, a common disorder of the peripheral nervous system, caused by demyelination or axonal degeneration or a combination of both, mutant families analysis, mutation analysis, phenotype, overview
additional information
two closely related, internally deleted, splice variants of homodimeric human tyrosyl-tRNA synthetase (TyrRS) are analyzed, in spite of both variants ablating a portion of the catalytic core and dimer-interface contacts of native TyrRS, each folded into a distinct stable structure. The internal deletion of TyrRSE2-4 splice variant gives an alternative, neomorphic dimer interface orthogonal to that of native TyrRS. One splice variant, TyrRSE2-4, is largely dimeric while the other is mostly monomeric. TyrRS SVs are specifically enriched in lymphocytes and lung tissue
additional information
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two closely related, internally deleted, splice variants of homodimeric human tyrosyl-tRNA synthetase (TyrRS) are analyzed, in spite of both variants ablating a portion of the catalytic core and dimer-interface contacts of native TyrRS, each folded into a distinct stable structure. The internal deletion of TyrRSE2-4 splice variant gives an alternative, neomorphic dimer interface orthogonal to that of native TyrRS. One splice variant, TyrRSE2-4, is largely dimeric while the other is mostly monomeric. TyrRS SVs are specifically enriched in lymphocytes and lung tissue
additional information
gene deletion mutations are attempted via targeted gene replacement. The heterozygous mutants show slower growth kinetics and exhibited attenuated virulence. LdTyrRS chromosomal null mutants do not survive. Single allele of the LdTyrRS gene is replaced in heterozygous mutant parasites (TyrRS/HYG or TyrRS/NEO), leading to 1.8fold decreased expression of TyrRS protein in heterozygous mutants (TyrRS/HYG)
additional information
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gene deletion mutations are attempted via targeted gene replacement. The heterozygous mutants show slower growth kinetics and exhibited attenuated virulence. LdTyrRS chromosomal null mutants do not survive. Single allele of the LdTyrRS gene is replaced in heterozygous mutant parasites (TyrRS/HYG or TyrRS/NEO), leading to 1.8fold decreased expression of TyrRS protein in heterozygous mutants (TyrRS/HYG)
additional information
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gene deletion mutations are attempted via targeted gene replacement. The heterozygous mutants show slower growth kinetics and exhibited attenuated virulence. LdTyrRS chromosomal null mutants do not survive. Single allele of the LdTyrRS gene is replaced in heterozygous mutant parasites (TyrRS/HYG or TyrRS/NEO), leading to 1.8fold decreased expression of TyrRS protein in heterozygous mutants (TyrRS/HYG)
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additional information
computational design of possible mutants with altered substrate specificity by prediction of the binding structure and calculation of binding energies of mutants to amino acids, overview
additional information
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computational design of possible mutants with altered substrate specificity by prediction of the binding structure and calculation of binding energies of mutants to amino acids, overview
additional information
structural comparison of wild-type enzyme and naturally occuring mutant variant p-BrPhe TyrRSs, the latter shows an altered substrate specificity charging 4-bromophenylalanine, 3-(2-naphthyl)alanine, or 4-acetylphenylalanine, overview
additional information
60 aminoacyl-tRNA synthetases are modeled using the conformation of Methanococcus jannaschii tRNATyr/tyrosyl-tRNA synthetase as template
additional information
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60 aminoacyl-tRNA synthetases are modeled using the conformation of Methanococcus jannaschii tRNATyr/tyrosyl-tRNA synthetase as template
additional information
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the Escherichia coli TyrRS-tRNATyr pair is functionally replaced by the Methanocaldococcus jannaschii tyrosine pair
additional information
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development of a one-plasmid expression system encoding an inducible modified tyrosyl-tRNA synthetase, the orthogonal cognate suppressor tRNA, and eGFPUAG in an individually regulatable fashion, overview. Assessment of the system for the incorporation of a non-natural amino acid yielding a fluorescent readout. Mutant library construction by random mutagenesis, and selection for O-methyl-L-tyrosine-specific mutant variants
additional information
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mutation of the ELR-motif to EYR abolishes the effect on ischemic angiogenesis, leukocyte recruitment, and vascular permeability
additional information
prevention of beta-sheet formation by introducing point mutations in the loop sequence results in a rapid transition (below 20 ns) of the loop from its functional closed M-like structure to an inactive open O-like structure, i.e. rapid diffusion of the catalytic loop outside the active site
additional information
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prevention of beta-sheet formation by introducing point mutations in the loop sequence results in a rapid transition (below 20 ns) of the loop from its functional closed M-like structure to an inactive open O-like structure, i.e. rapid diffusion of the catalytic loop outside the active site
additional information
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prevention of beta-sheet formation by introducing point mutations in the loop sequence results in a rapid transition (below 20 ns) of the loop from its functional closed M-like structure to an inactive open O-like structure, i.e. rapid diffusion of the catalytic loop outside the active site
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additional information
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construction of diverse tRNA variants of the native tRNATyr from yeast by heterologous in vitro translation, transplantation and point mutations
additional information
construction of a chemically truncated enzyme comprising residues 1-364, termed SceTyrRS
additional information
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construction of a chemically truncated enzyme comprising residues 1-364, termed SceTyrRS
additional information
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the Escherichia coli TyrRS-tRNATyr pair is functionally replaced by the Saccharomyces cerevisiae tyrosine pair
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a library of more than 200 mutants substituting the ATP binding motif KMSSS, Lys204-Met205-Ser206-Ser207-Ser208, is built, mutants and wild-type of MjYRS are cloned into the vector pET41a+
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catalytic domain (residues 1-322)
CYT-18 is expressed from the plasmid pEX560 in the Escherichia coli strain HMS174DE3
DNA and amino acid sequence determination and analysis of two enzymes types, expression of tyrosyl aminoacyl-tRNA synthetase as C-terminally His6-tagged enzyme in Escherichia coli
DNA and amino acid sequence determination and analysis, RT-PCR expression analysis, phylogenetic analysis and tree
DNA and amino acid sequence determination of wild-type and mutant enzymes, localization of the gene encoding the enzyme on chromosome 1p34-p35, functional complementation of a Saccharomyces cerevisiae TYS1 mutant strain, overview, transient expression of EGFP-tagged wild-type and mutant enzymes in murine neuroblastoma N2a cells
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expressed in Escherichia coli
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL cells
expression in Escherichia coli
expression in Escherichia coli strain BL21(DE3)
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expression of C-terminal domain of TyrRS in Escherichia coli strain BL21(DE3)
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expression of His-tagged full-length wild-type and truncated mutant enzymes in Escherichia coli
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expression of the enzyme as His-tagged protein in Escherichia coli strain BL21(DE3)
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expression of truncated enzyme SceTyrRS comprising residues 1-364
expression of wild-type and mutant enzymes as His-tagged proteins in Escherichia coli
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for expression in Escherichia coli TG2 cells
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gene EGW00102, sequence comparisons, recombinant expression of codon-optimized His6-tagged enzyme in Escherichia coli strain BL21(DE3), recombinant expression of the enzyme ligated to a ribozyme for in vitro transcription by T7 polymerase
gene structure and motifs in double-length TyrRS homologues, phylogenetic comparison
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gene TyrS, DNA sequence determination, overexpression as His-tagged enzyme in Escherichia coli BL21
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gene tyrS, expression of wild-type and mutant enzymes as His-tagged proteins in strain JM109
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gene tyrS, overexpression of wild-type and mutant enzymes from phage M13-BY(DELTA1) in Escherichia coli strains RZ1032 and TG2
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gene tyrS, recombinant expression of His-tagged wild-type enzyme in Escherichia coli strain BL21(DE3), recombinant expression of His-tagged mutant enzymes in Saccharomyces cerevisiae strain BY4742
gene tyrS, recombinant expression of His6-tagged wild-type enzyme and site-specifically acetylated TyrRS variants in Escherichia coli strain BL21(DE3) cells
gene tyrS, sequence comparisons, single copy gene, recombinant expression of N-terminally His6-tagged enzyme, overexpression of wild-type and mutant enzymes LdTyrRS
gene tyrZ, overexpression of the HIs-tagged enzyme in Escherichia coli strain JM105
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into the pUAST transformation vector
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into the single copy plasmid YCplac111
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into the TOPO TA cloning vector for sequencing
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into the vectors pACYC184 and pAp102
mutant human mini-TyrRS constructs are generated using QuikChange site-directed mutagenesis kit and using a plasmid encoding the gene for wild-type human mini-TyrRS as the template for PCR mutagenesis reactions, all proteins are expressed with a C-terminal His-tag to facilitate purification
overexpression in Escherichia coli
overexpression of His-tagged wild-type and mutant Y43G enzyme in Escherichia coli BL21(DE3)
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overexpression of His-tagged wild-type and mutants in strain BL21(DE3)
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recombinant expression of His-tagged enzyme in Escherichia coli from AVA0421 vector
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recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
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recombinant overexpression in Escherichia coli
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TyrRS, phylogenetic analysis, the viral aminoacyl tRNA synthetases have not been acquired recently by horizontal gene transfer from a cellular host but rather militate in favor of an intricate evolutionary relationship between large DNA viruses and ancestral eukaryotes
tyrS, DNA and amino acid sequence determination and analysis, analysis of two closely related, internally deleted, splice variants of homodimeric human tyrosyl-tRNA synthetase (TyrRS). Detection of the TyrRS transcripts in the cytoplasmic and polyribosomal RNA is carried out by PCR using primers targeting the 5'-UTR/exon1 and exon5/exon6 regions of the TyrRS gene (FP and RP2). Recombinant expression of splice variants in Jurkat T, THP-1, or HEK-293T cells, and recombinant expression of splice variants as thioredoxin-His-tagged proteins in Escherichia coli strain BL21(DE3), removal of the tag by protease-3C, followed by gel filtration
wild-type and mutants into the phagemid pYTS5-WT
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-
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expressed in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Escherichia coli as a His-tagged fusion protein
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expressed in Escherichia coli as a His-tagged fusion protein
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expressed in Escherichia coli as a His-tagged fusion protein
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expression in Escherichia coli
expression in Escherichia coli
into the vectors pACYC184 and pAp102
-
into the vectors pACYC184 and pAp102
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into the vectors pACYC184 and pAp102
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