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2,3-dihydroxybenzoate + O2
CO2 + alpha-hydroxymuconic semialdehyde
-
-
mutant H200F produces alpha-carboxy-cis,cis-muconic acid
-
?
3,4 dihydroxyphenylacetate + O2
1-carboxymethyl-4-hydroxy-cis-muconic semialdehyde
-
-
-
-
?
3,4-dihydroxybenzoic acid + O2
2-hydroxy-5-carboxymuconate semialdehyde
3,4-dihydroxymandelate + O2
?
3,4-dihydroxyphenylacetate + O2
1-carboxymethyl-4-hydroxy-cis-muconic semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethyl-cis,cis-muconate semialdehyde
-
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
3,4-dihydroxyphenylacetate + O2
?
3,4-dihydroxyphenylpropionate + O2
2-hydroxy-5-carboxyethylmuconate semialdehyde
3-(3,4-dihydroxyphenyl)-DL-alanine + O2
(2E,4Z)-7-amino-5-formyl-2-hydroxyocta-2,4-dienedioic acid
-
-
-
-
?
4-nitrocatechol + O2
(2Z,4Z)-2-hydroxy-4-nitro-6-oxohexa-2,4-dienoate
-
-
-
?
4-nitrocatechol + O2
(2Z,4Z)-2-hydroxy-5-nitro-6-oxohexa-2,4-dienoate
-
-
-
?
N-formyl-3-(3,4-dihydroxyphenyl)-DL-alanine + O2
(2E,4Z)-5-formyl-7-(formylamino)-2-hydroxyocta-2,4-dienedioic acid
-
-
-
-
?
additional information
?
-
3,4-dihydroxybenzoic acid + O2
2-hydroxy-5-carboxymuconate semialdehyde
-
0.58% of the activity with 3,4-dihydroxyphenylacetate
-
-
?
3,4-dihydroxybenzoic acid + O2
2-hydroxy-5-carboxymuconate semialdehyde
-
-
-
-
?
3,4-dihydroxybenzoic acid + O2
2-hydroxy-5-carboxymuconate semialdehyde
-
0.125% of the activity with 3,4-dihydroxyphenylacetate
-
-
?
3,4-dihydroxymandelate + O2
?
Arthrobacter synephrinum
-
50% of the activity with 3,4-dihydroxyphenylacetate
-
-
?
3,4-dihydroxymandelate + O2
?
-
14% of the activity with 3,4-dihydroxyphenylacetate
-
-
?
3,4-dihydroxymandelate + O2
?
-
83% of the activity with 3,4-dihydroxyphenylacetate
-
-
?
3,4-dihydroxymandelate + O2
?
-
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
enzyme is induced by 4-hydroxyphenylacetate
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
enzyme is involved in the meta-cleavage pathway for the degradation of 4-hydroxyphenylacetic acid
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
enzyme is involved in the meta-cleavage pathway for the degradation of 4-hydroxyphenylacetic acid
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
enzyme is involved in catabolism of L-Tyr
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
Arthrobacter synephrinum
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
enzyme catalyzes the estradiol cleavage of catechols
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
key ring cleavage step in metabolism of 3,4-dihydroxyphenylacetate
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
proximal extradiol cleavage of the aromatic ring of the substrate
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
Fe2+-containing homoprotocatechuate 2,3-dioxygenase, FeHPCD, activates O2 to catalyze the aromatic ring opening of homoprotocatechuate. O2 activation steps for extradiol dioxygenases, mechanism, overview
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
Mössbauer spectra of the reaction intermediates trapped by rapid freeze quench show that both intermediates contain Fe2+. The lack of a chromophore characteristic of a quinone or semiquinone form of HPCA, the presence of Fe2+, and the low O2 affinity suggests that is an HPCA-FeII-O2 complex with little electron delocalization onto the O2
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
substrates homoprotocatechuate and O2 bind to the Fe2+ of homoprotocatechuate 2,3-dioxygenase in adjacent coordination sites. Transfer of an electron(s) from 3,4-dihydroxyphenylacetate to O2 via the iron is proposed to activate the substrates for reaction with each other to initiate aromatic ring cleavage. Oxygen is bound as a (hydro)peroxo ligand. At least four intermediates form following addition of O2 with a pre-formed enzyme-substrate complex, different intermediate formation in mutant H200N, Mössbauer spectral analysis, overview
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
inducible enzyme
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
enzyme is involved in catabolism of L-Tyr
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
catabolism of 3-hydroxyphenylacetate and 4-hydroxyphenylacetate by 3,4-dihydroxyphenylacetate pathway
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
enzyme is involved in catabolism of L-Tyr
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
enzyme is involved in catabolism of biogenic amines
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
the enzyme catalyzes the extradiol ring cleavage of 3,4-dihydroxyphenylacetate (DHPA) by incorporation of molecular oxygen to yield 5-carboxymethyl-2-hydroxymuconate semialdehyde (CHMS). O2 insertion occurs through the substrate-alkylperoxo-Fe(II) intermediate
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
the enzyme catalyzes the extradiol ring cleavage of 3,4-dihydroxyphenylacetate (DHPA) by incorporation of molecular oxygen to yield 5-carboxymethyl-2-hydroxymuconate semialdehyde (CHMS). O2 insertion occurs through the substrate-alkylperoxo-Fe(II) intermediate
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
induced by 3,4-dihydroxyphenylacetate
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
induced by 3-chlorophenylacetate
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
induced by 3-chlorophenylacetate
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
?
-
1 mM, assay at pH 7.8, 23°C
-
-
?
3,4-dihydroxyphenylacetate + O2
?
-
1 mM, assay at pH 7.8, 23°C
-
-
?
3,4-dihydroxyphenylpropionate + O2
2-hydroxy-5-carboxyethylmuconate semialdehyde
Arthrobacter synephrinum
-
4% of the activity with 3,4-dihydroxyphenylacetate
-
-
?
3,4-dihydroxyphenylpropionate + O2
2-hydroxy-5-carboxyethylmuconate semialdehyde
-
5% of the activity with 3,4-dihydroxyphenylacetate
-
-
?
3,4-dihydroxyphenylpropionate + O2
2-hydroxy-5-carboxyethylmuconate semialdehyde
-
58% of the activity with 3,4-dihydroxyphenylacetate
-
-
?
3,4-dihydroxyphenylpropionate + O2
2-hydroxy-5-carboxyethylmuconate semialdehyde
-
2.86% of the activity with 3,4-dihydroxyphenylacetate
-
-
?
3,4-dihydroxyphenylpropionate + O2
2-hydroxy-5-carboxyethylmuconate semialdehyde
-
low activity
-
-
?
4-nitrocatechol + O2
?
-
-
-
?
4-nitrocatechol + O2
?
-
-
cleavage in proximal extradiol position
-
?
4-nitrocatechol + O2
?
-
a slow alternative substrate
-
-
?
4-nitrocatechol + O2
?
-
not the native substrate for HPCD, it is cleaved in a similar fashion as the natural substrate, homoprotocatechuate, 4-nitrocatechol exhibits characteristic visible absorption bands that are sensitive to its ionization and oxidation states, suitable for spectral substrate binding and reaction mechanism analysis
-
-
?
additional information
?
-
-
enzyme also has catalase activity
-
-
?
additional information
?
-
-
LB400 cells grown with 3-hydroxyphenylacetate degrade homoprotocatechuate and show homoprotocatechuate 2,3-dioxygenase activity
-
-
?
additional information
?
-
-
poor or no activity with 3,4-dihydroxyphenylpropionate, 3,4-dihydroxybenzoate, 4-hydroxyphenylacetate, 4-hydroxybenzoate, 4-hydroxyphenylpropionate, 4-hydroxy-3-methoxyphenylacetate, and 4-nitrocatechol
-
-
?
additional information
?
-
-
poor or no activity with 3,4-dihydroxyphenylpropionate, 3,4-dihydroxybenzoate, 4-hydroxyphenylacetate, 4-hydroxybenzoate, 4-hydroxyphenylpropionate, 4-hydroxy-3-methoxyphenylacetate, and 4-nitrocatechol
-
-
?
additional information
?
-
-
very low activity with various 4-substituted catechols
-
-
?
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3,4 dihydroxyphenylacetate + O2
1-carboxymethyl-4-hydroxy-cis-muconic semialdehyde
-
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
additional information
?
-
-
LB400 cells grown with 3-hydroxyphenylacetate degrade homoprotocatechuate and show homoprotocatechuate 2,3-dioxygenase activity
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
enzyme is induced by 4-hydroxyphenylacetate
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
enzyme is involved in the meta-cleavage pathway for the degradation of 4-hydroxyphenylacetic acid
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
enzyme is involved in the meta-cleavage pathway for the degradation of 4-hydroxyphenylacetic acid
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
enzyme is involved in catabolism of L-Tyr
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
enzyme catalyzes the estradiol cleavage of catechols
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
key ring cleavage step in metabolism of 3,4-dihydroxyphenylacetate
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
inducible enzyme
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
enzyme is involved in catabolism of L-Tyr
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
catabolism of 3-hydroxyphenylacetate and 4-hydroxyphenylacetate by 3,4-dihydroxyphenylacetate pathway
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
enzyme is involved in catabolism of L-Tyr
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
enzyme is involved in catabolism of biogenic amines
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
induced by 3,4-dihydroxyphenylacetate
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
-
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
induced by 3-chlorophenylacetate
-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
-
induced by 3-chlorophenylacetate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.074 - 0.45
3,4-dihydroxybenzoic acid
0.5
3,4-dihydroxymandelate
Arthrobacter synephrinum
-
-
0.0004 - 0.067
3,4-Dihydroxyphenylacetate
0.0037
3,4-Dihydroxyphenylpropionic acid
-
32°C
0.015
4-nitrocatechol
-
pH 7.5, 22°C
0.035
DL-3,4-dihydroxymandelic acid
-
32°C
additional information
additional information
-
Michaelis-Menten steady-state kinetics under air-saturated conditions. The rate determining steps of the PaDHPAO reaction at temperatures above and below 35°C may be different
-
0.074
3,4-dihydroxybenzoic acid
-
-
0.45
3,4-dihydroxybenzoic acid
-
-
0.0004
3,4-Dihydroxyphenylacetate
-
24°C, pH 7.5, mutant enzyme H200E
0.0034
3,4-Dihydroxyphenylacetate
-
32°C
0.004
3,4-Dihydroxyphenylacetate
-
28°C
0.0047
3,4-Dihydroxyphenylacetate
-
21°C
0.005
3,4-Dihydroxyphenylacetate
-
24°C, pH 7.5, mutant enzyme H200A
0.0058
3,4-Dihydroxyphenylacetate
-
38°C
0.0074
3,4-Dihydroxyphenylacetate
-
47°C
0.01
3,4-Dihydroxyphenylacetate
-
24°C, pH 7.5, mutant enzyme H20N
0.011
3,4-Dihydroxyphenylacetate
-
recombinant enzyme
0.012
3,4-Dihydroxyphenylacetate
-
23°C, pH 7.5, mutant enzyme H200A
0.014
3,4-Dihydroxyphenylacetate
-
Mn-MndD
0.015
3,4-Dihydroxyphenylacetate
-
-
0.015
3,4-Dihydroxyphenylacetate
-
Fe-MndD
0.016
3,4-Dihydroxyphenylacetate
-
-
0.017
3,4-Dihydroxyphenylacetate
-
23°C, pH 7.5, mutant enzyme H200E
0.018
3,4-Dihydroxyphenylacetate
-
23°C, pH 7.5, mutant enzyme H200Q
0.021
3,4-Dihydroxyphenylacetate
-
23°C, pH 7.5, mutant enzyme H200N
0.021
3,4-Dihydroxyphenylacetate
-
23°C, pH 7.5, wild-type enzyme
0.025
3,4-Dihydroxyphenylacetate
-
-
0.025
3,4-Dihydroxyphenylacetate
Arthrobacter synephrinum
-
-
0.025
3,4-Dihydroxyphenylacetate
-
pH 7.5, 22°C
0.028
3,4-Dihydroxyphenylacetate
-
24°C, pH 7.5, mutant enzyme H200Q
0.03
3,4-Dihydroxyphenylacetate
-
24°C, pH 7.5, wild-type enzyme
0.031
3,4-Dihydroxyphenylacetate
-
24°C, pH 7.5, mutant enzyme H200F
0.031
3,4-Dihydroxyphenylacetate
-
Fe-HPCD
0.035
3,4-Dihydroxyphenylacetate
-
Mn-HPCD
0.058
3,4-Dihydroxyphenylacetate
-
pH 7.5, 25°C, in presence of ascorbate
0.067
3,4-Dihydroxyphenylacetate
-
pH 7.5, 25°C
0.037
O2
-
Fe-MndD
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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.
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E266Q
-
specific activity is less than 0.1% of that of the wild-type enzyme, binds 33% of the wild-type level of manganese
H155A
-
specific activity is less than 0.1% of that of the wild-type enzyme, binds 0.4% of the wild-type level of manganese
H200A
-
KM-value for 3,4-dihydroxyphenylacetate is 1.75fold lower than wild-type value, kcat for 3,4-dihydroxyphenylacetate is 69fold lower than wild-type value
H200E
-
KM-value for 3,4-dihydroxyphenylacetate is 1.2fold lower than wild-type value, kcat for 3,4-dihydroxyphenylacetate is more than 276fold lower than wild-type value, Mn content per monomer is 2fold lower than in wild-type enzyme
H200N
-
KM-value for 3,4-dihydroxyphenylacetate is identical to wild-type value, kcat for 3,4-dihydroxyphenylacetate is 1.73fold lower than wild-type value, Mn content per monomer is 65% of wild-type value
H200Q
-
KM-value for 3,4-dihydroxyphenylacetate is 1.2fold lower than wild-type value, kcat for 3,4-dihydroxyphenylacetate is 1.3fold lower than wild-type value
H214A
-
specific activity is less than 0.1% of that of the wild-type enzyme, binds 1.8% of the wild-type level of manganese
H42A
-
97% of wild-type activity at 18°C, 30% of wild-type activity at 37°C
E266Q
-
specific activity is less than 0.1% of that of the wild-type enzyme, binds 33% of the wild-type level of manganese
-
H155A
-
specific activity is less than 0.1% of that of the wild-type enzyme, binds 0.4% of the wild-type level of manganese
-
H200A
-
KM-value for 3,4-dihydroxyphenylacetate is 1.75fold lower than wild-type value, kcat for 3,4-dihydroxyphenylacetate is 69fold lower than wild-type value
-
H200E
-
KM-value for 3,4-dihydroxyphenylacetate is 1.2fold lower than wild-type value, kcat for 3,4-dihydroxyphenylacetate is more than 276fold lower than wild-type value, Mn content per monomer is 2fold lower than in wild-type enzyme
-
H200N
-
KM-value for 3,4-dihydroxyphenylacetate is identical to wild-type value, kcat for 3,4-dihydroxyphenylacetate is 1.73fold lower than wild-type value, Mn content per monomer is 65% of wild-type value
-
H200Q
-
KM-value for 3,4-dihydroxyphenylacetate is 1.2fold lower than wild-type value, kcat for 3,4-dihydroxyphenylacetate is 1.3fold lower than wild-type value
-
H214A
-
specific activity is less than 0.1% of that of the wild-type enzyme, binds 1.8% of the wild-type level of manganese
-
H42A
-
97% of wild-type activity at 18°C, 30% of wild-type activity at 37°C
-
H200A
-
Km-value for 3,4-dihydroxyphenylacetate is 6fold lower than wild-type value, kcat for 3,4-dihydroxyphenylacetate is 33.3fold lower than wild-type value
H200E
-
Km-value for 3,4-dihydroxyphenylacetate is 75fold lower than wild-type value, kcat for 3,4-dihydroxyphenylacetate is 11.1fold lower than wild-type value
H200Q
-
Km-value for 3,4-dihydroxyphenylacetate is similar to wild-type value, kcat for 3,4-dihydroxyphenylacetate is 2.5fold lower than wild-type value
H200F
-
switch of reaction from extradiol to intradiol cleavage for substrate 2,3-dihydroxybenzoate
H200F
-
Km-value for 3,4-dihydroxyphenylacetate is similar to wild-type value, kcat for 3,4-dihydroxyphenylacetate is 47.6fold lower than wild-type value
H200N
-
active site mutant
H200N
-
Km-value for 3,4-dihydroxyphenylacetate is 3fold lower than wild-type value, kcat for 3,4-dihydroxyphenylacetate is 3.33fold lower than wild-type value
H200N
-
site-directed mutagenesis, catalytic reaction intermediate formation in the mutant differs from the wild-type enzyme, Mössbauer spectral analysis, overview
H200N
variant employs a C4 (para-carbon) pathway to produce a C4-C5 cleavage product
Y257F
site-directed mutagenesis, changes in kinetics for Y257F variant can be attributed to the loss of interactions between substrate and Tyr257, substrate binding structures compared to the wild-type enzyme, overview
Y257F
-
site-directed mutagenesis, the two reaction intermediates formed with the mutant enzyme differ from that of the the wild-type enzyme, substrate binds tightly to Y257F, the intense Mössbauer spectrum of suggests the intermediate is most likely an HPCA quinone-FeII-(hydro)peroxo species. Steady-state and transient kinetic analyses show that steps of the catalytic cycle are slowed by as much as 100fold by the mutation due to failure of Y257F to facilitate the observed distortion of the bound HPCA that is proposed to promote transfer of one electron to O2, Mössbauer spectral analysis, overview
additional information
-
triple mutant in which the three gaps in the sequence are removed does not show a significant change in metal content
additional information
small model including only the most relevant parts of the residues, H155, H214, E267, Y257, directyl coordinated to Fe(II); model insufficient for a proper modeling of the enzymatic reaction
additional information
-
small model including only the most relevant parts of the residues, H155, H214, E267, Y257, directyl coordinated to Fe(II); model insufficient for a proper modeling of the enzymatic reaction
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