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acetyl-CoA + H2O + 2-oxoadipate
2-hydroxyhexane-1,2,6-tricarboxylate
-
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
(2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
acetyl-CoA + H2O + 2-oxoglutarate
(R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
acetyl-CoA + H2O + oxaloacetate
2-hydroxypropane-1,2,3-tricarboxylate + CoA
acetyl-CoA + H2O + oxaloacetate
?
-
oxaloacetate is a slow alternative substrate
-
-
?
acetyl-CoA + H2O + oxaloacetate
? + CoA
-
oxaloacetate is a substrate with lower affinity than 2-oxoglutarate
-
-
?
additional information
?
-
acetyl-CoA + H2O + 2-oxoglutarate
(2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
(2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
(2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
(2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
(2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
(2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
(2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
the enzyme catalyzes the first and committed step of the alpha-aminoadipate pathway
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
(2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
(2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
the enzyme catalyzes the first and committed step of the alpha-aminoadipate pathway
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
(R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
(R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
(R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
(R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
specific substrates
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
specific substrates
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
enzymatic formation of homocitric acid, an intermediate in lysine biosynthesis
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
expression of lys1 is partially repressed by high concentrations of lysine in the culture medium, but lysine repression seems to be a weak mechanism of control of the lysine pathway as compared to lysine inhibition of homocitrate synthase
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
the enzyme catalyzes the first step of the lysine and penicillin pathway and is highly sensitive to feedback regulation by L-lysine
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
the enzyme may play a regulatory function, in addition to its catalytic function, in Saccharomyces cerevisiae but not in Penicillium chrysogenum
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
first enzyme of the lysine biosynthetic pathway, feedback regulated by L-lysine. Maximum homocitrate synthase activity in cultures is found at 48 h, coinciding with the phase of high rate of penicillin biosynthesis
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
the enzyme may play a regulatory function, in addition to its catalytic function, in Saccharomyces cerevisiae but not in Penicillium chrysogenum
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
first enzyme of the 2-aminoadipic acid pathway for biosynthesis of lysine
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
sequential ordered kinetic mechanism for the histidine-tagged enzyme with 2-oxoglutarate binding before acetyl-CoA and CoA released before homocitrate
-
-
ir
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
in the yeast Saccharomyces cerevisiae, the first committed step of the lysine biosynthetic pathway is catalysed by two homocitrate synthases encoded by LYS20 and LYS21. During growth on ethanol, homocitrate is mainly synthesized through Lys21p, while under fermentative metabolism, Lys20p and Lys21p play redundant roles
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
a catalytic dyad comprising Glu155 and His309 acts to deprotonate the methyl group of acetyl-CoA, while Tyr320 is likely not directly involved in catalysis, but may aid in orienting the reactant and/or the catalytic dyad
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
Saccharomycopsis lipolytica
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
first enzyme of the lysine biosynthetic pathway
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
first enzyme of the lysine biosynthetic pathway
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
2-hydroxypropane-1,2,3-tricarboxylate + CoA
-
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
2-hydroxypropane-1,2,3-tricarboxylate + CoA
-
-
-
-
?
additional information
?
-
-
isoforms Lys21p and Lys22p are not able to catalyze the condensation of oxaloacetate with acetyl-CoA to give citrate
-
-
?
additional information
?
-
-
the enzyme has no activity with core histone substrates or calf thymus histones. However, when histone H4 purified from yeast is used as substrate, histone acetyltransferases activity is observed
-
-
?
additional information
?
-
-
homocitrate synthase is a labile target for oxidative stress caused by CuZn-superoxide dismutase depletion
-
-
?
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acetyl-CoA + H2O + 2-oxoglutarate
(2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
acetyl-CoA + H2O + 2-oxoglutarate
(R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
additional information
?
-
-
homocitrate synthase is a labile target for oxidative stress caused by CuZn-superoxide dismutase depletion
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
(2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
(2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
(2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
(2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
the enzyme catalyzes the first and committed step of the alpha-aminoadipate pathway
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
(2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
the enzyme catalyzes the first and committed step of the alpha-aminoadipate pathway
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
(R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
(R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
(R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
(R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
enzymatic formation of homocitric acid, an intermediate in lysine biosynthesis
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
expression of lys1 is partially repressed by high concentrations of lysine in the culture medium, but lysine repression seems to be a weak mechanism of control of the lysine pathway as compared to lysine inhibition of homocitrate synthase
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
the enzyme catalyzes the first step of the lysine and penicillin pathway and is highly sensitive to feedback regulation by L-lysine
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
the enzyme may play a regulatory function, in addition to its catalytic function, in Saccharomyces cerevisiae but not in Penicillium chrysogenum
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
first enzyme of the lysine biosynthetic pathway, feedback regulated by L-lysine. Maximum homocitrate synthase activity in cultures is found at 48 h, coinciding with the phase of high rate of penicillin biosynthesis
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
the enzyme may play a regulatory function, in addition to its catalytic function, in Saccharomyces cerevisiae but not in Penicillium chrysogenum
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
first enzyme of the 2-aminoadipic acid pathway for biosynthesis of lysine
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
in the yeast Saccharomyces cerevisiae, the first committed step of the lysine biosynthetic pathway is catalysed by two homocitrate synthases encoded by LYS20 and LYS21. During growth on ethanol, homocitrate is mainly synthesized through Lys21p, while under fermentative metabolism, Lys20p and Lys21p play redundant roles
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
first enzyme of the lysine biosynthetic pathway
-
-
?
acetyl-CoA + H2O + 2-oxoglutarate
2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
first enzyme of the lysine biosynthetic pathway
-
-
?
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1,10-phenanthroline
-
0.01 mM, 91% inhibition
2,2'-dipyridyl
-
0.01 mM, 82% inhibition
2-aminoethyl-L-cysteine
-
-
2-methylcitrate
89.6% residual activity at 5 mM
AMP
-
1 mM, 13-15% inhibition
benzylpenicillin
-
20 mM, partial inhibition is enhanced by lysine
Ca2+
96.3% residual activity at 1 mM
casein hydrolysate
-
about 50% inhibition
-
desulfo-CoA
-
uncompetitive
dipicolinic acid
Saccharomycopsis lipolytica
-
non-competitive inhibitor of 2-oxoglutarate fixation
dipyridyl
95% residual activity at 0.1 mM
DL-4,5-transdehydrolysine
Saccharomycopsis lipolytica
-
5 mM, 90% inhibition
DL-allo-5-Hydroxylysine
Saccharomycopsis lipolytica
-
5 mM, 75% inhibition
DL-alpha-aminoadipate
-
-
DL-alpha-Difluoromethyllysine
-
strong inhibitor of isoform Lys22p, but not Lys21p
DL-Homolysine
-
inhibition of enzyme from wild-type strain, enzyme from S-(beta-aminoethyl)-L-cysteine resistant mutant strain is not inhibited
glyoxylate
-
competitive, analysis of pH-dependence of inhibition
iodoacetic acid
-
0.01 mM, 71% inhibition
K+
91.7% residual activity at 0.1 mM
LL-Diaminopimelic acid
Saccharomycopsis lipolytica
-
5 mM, 90% inhibition
Mg2+
-
10 mM MgSO4, 30% inhibition
Na2HAsO4
-
0.01 mM, 67% inhibition
Na2SO4
90.9% residual activity at 0.2 mM
NaF
-
0.01 mM, 73% inhibition
NEM
-
0.1 mM, 90% inhibition
oxalglycine
-
competitive inhibition versus 2-oxoglutarate
p-hydroxymercuribenzoate
-
0.0001 mM, complete inhibition
pipecolic acid
Saccharomycopsis lipolytica
-
non-competitive inhibition on the fixation of both substrates
pyridine-2,3-dicarboxylate
-
-
Pyridine-2,4-dicarboxylate
-
-
Pyridine-2,5-dicarboxylate
-
-
pyridine-2,6-dicarboxylate
-
-
pyridine-2-carboxylate
-
-
S-(2-aminoethyl)-L-cysteine
-
-
S-(beta-aminoethyl)-L-cysteine
-
1.1 mM required for half-maximal inhibition of enzyme from wild-type strain, enzyme from S-(beta-aminoethyl)-L-cysteine resistant mutant strain is not inhibited
Selenalysine
-
7.5 mM, 90% inhibition, half-maximal inhibition at 1.9 mM, competitive inhibition against both acetyl-CoA and 2-oxoglutarate
citrate
66.1% residual activity at 10 mM
citrate
-
competitive versus 2-oxoglutarate; noncompetitive
CoA
-
-
CoA
-
noncompetitive versus acetyl-CoA
CoA
Saccharomycopsis lipolytica
-
strong competitive inhibitor of acetyl-CoA fixation
CoA
-
in the presence of Mg2+, or Mn2+, product inhibition by CoA is competitive versus acetyl-CoA but uncompetitive versus 2-oxoglutarate
Cu2+
0.7% residual activity at 0.025 mM
Cu2+
-
strong inhibitory effect on isoform Lys22p
Cu2+
-
0.0001 mM CuSO4, complete inhibition
EDTA
13.4% residual activity at 5 mM
EDTA
-
strong inhibitory effect on isoform Lys22p
EDTA
-
5 mM, 30% inhibition
EDTA
Saccharomycopsis lipolytica
-
15 mM
Hg2+
-
-
Hg2+
-
0.01 mM HgCl2, complete inhibition
hydroxylysine
-
20 mM, 69% inhibition
hydroxylysine
-
DL-hydroxylysine
L-Arg
-
inhibitor of isoform Lys22p, but not Lys21p
L-Lys
-
competitive inhibitor
L-Lys
-
0.3 mM, 50% inhibition
L-Lys
-
50 mM, 48% inhibition. Feed-back inhibition
L-Lys
-
50% inhibition by 0.053 mM, at 6 mM 2-oxoglutarate
L-Lys
-
20 mM, 95% inhibition
L-Lys
-
10 mM, 80% inhibition. No inhibition by 10 mM D-Lys
L-Lys
-
feedback inhibition of homocitrate synthase by lysine modulates the activation of LYS gene expression by transcriptional activator Lys14p
L-Lys
Saccharomycopsis lipolytica
-
5 mM, complete inhibition
L-Lys
-
0.02 mM required for half-maximal inhibition of the enzyme from wild-type strain, enzyme from S-(beta-aminoethyl)-L-cysteine resistant mutant strain is not inhibited
L-lysine
24.4% residual activity at 50 mM
L-lysine
-
isoform Lys20 is one order of magnitude less sensitive to L-lysine inhibition than Lys21
L-lysine
feedback inhibition
L-lysine
-
competitive inhibitor versus 2-oxoglutarate up to a concentration of 1 mM
Lys
-
feedback inhibitor, competitive versus 2-oxoglutarate and linear in the physiological range of lysine concentrations up to 5 mM
Lys
-
binding to the less active enzyme conformer
lysine
strong allosteric inhibitor of Lys21p. Induces positive cooperativity for alpha-ketoglutarate binding
lysine
mutant enzyme lacking the RAM domain is insensitive to inhibition by lysine
lysine
-
regulated via feedback inhibition by the endproduct
Mn2+
-
-
Mn2+
-
0.025 mM, 35% inhibition
Na+
-
activator at low concentrations, inhibitor at high concentrations, inhibition and activation can occur simultaneously, inhibition by Na+ is eliminated at high concentrations of acetyl-CoA
Na+
-
activity is simultaneously inhibited and activated. Activation by Na+ binding to the active enzyme conformer at an allosteric site. Inhibition by binding to the active site
thialysine
-
L-thialysine
thialysine
-
5 mM, complete inhibition
thialysine
-
competitive with acetyl-CoA
Zn2+
0.8% residual activity at 0.1 mM
Zn2+
-
strong inhibitory effect on isoform Lys22p
Zn2+
-
0.025 mM, 60% inhibition
additional information
-
not inhibited by L-ornithine, L-norleucine, L-leucine, L-canavanine, gamma-amino-beta-hydroxybutyric acid, gamma-amino-n-butyric acid, and O-(2-aminoethyl)-L-serine; there is little or no effect of Mg2+ or Ca2+ ions
-
additional information
-
not inhibited by oxalate, malonyl-CoA, pantothenate
-
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Evidence for a catalytic dyad in the active site of homocitrate synthase from Saccharomyces cerevisiae
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Saccharomyces cerevisiae
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Quezada, H.; Aranda, C.; DeLuna, A.; Hernandez, H.; Calcagno, M.L.; Marin-Hernandez, A.; Gonzalez, A.
Specialization of the paralogue LYS21 determines lysine biosynthesis under respiratory metabolism in Saccharomyces cerevisiae
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Saccharomyces cerevisiae (P48570), Saccharomyces cerevisiae (Q12122), Saccharomyces cerevisiae
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Schizosaccharomyces pombe
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Schizosaccharomyces pombe (Q9Y823), Schizosaccharomyces pombe
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Lotus japonicus (D0VY45), Lotus japonicus
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Schoebel, F.; Jacobsen, I.D.; Brock, M.
Evaluation of lysine biosynthesis as an antifungal drug target: biochemical characterization of Aspergillus fumigatus homocitrate synthase and virulence studies
Eukaryot. Cell
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Aspergillus fumigatus (C7C437), Aspergillus fumigatus, Aspergillus fumigatus CBS 144.89 (C7C437)
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Homocitrate synthase connects amino acid metabolism to chromatin functions through Esa1 and DNA damage
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Saccharomyces cerevisiae
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Kumar, V.P.; West, A.H.; Cook, P.F.
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Thermus thermophilus
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Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
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Liu, F.; Wang, W.; Chen, B.Z.; Xie, B.G.
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Flammulina velutipes (M1U949), Flammulina velutipes, Flammulina velutipes W23 (M1U949)
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Gabriel, I.; Milewski, S.
Characterization of recombinant homocitrate synthase from Candida albicans
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Wang, J.; Wu, Y.; Sun, X.; Yuan, Q.; Yan, Y.
De novo biosynthesis of glutarate via alpha-keto acid carbon chain extension and decarboxylation pathway in Escherichia coli
ACS Synth. Biol.
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Saccharomyces cerevisiae (P48570), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P48570)
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Suzuki, T.; Akiyama, N.; Yoshida, A.; Tomita, T.; Lassak, K.; Haurat, M.F.; Okada, T.; Takahashi, K.; Albers, S.V.; Kuzuyama, T.; Nishiyama, M.
Biochemical characterization of archaeal homocitrate synthase from Sulfolobus acidocaldarius
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Sulfolobus acidocaldarius (Q4J989), Sulfolobus acidocaldarius DSM 639 (Q4J989)
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Hashimoto, S.; Wongdee, J.; Songwattana, P.; Greetatorn, T.; Goto, K.; Tittabutr, P.; Boonkerd, N.; Teaumroong, N.; Uchiumi, T.
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Bradyrhizobium sp. SUTN9-2, Bradyrhizobium sp. DOA9 (A0A0S6UXF5), Bradyrhizobium sp. ORS 285 (A0A1Y6KBA1)
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Nouwen, N.; Arrighi, J.F.; Cartieaux, F.; Chaintreuil, C.; Gully, D.; Klopp, C.; Giraud, E.
The role of rhizobial (NifV) and plant (FEN1) homocitrate synthases in Aeschynomene/photosynthetic Bradyrhizobium symbiosis
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Bradyrhizobium sp. ORS 285 (A0A1Y6KBA1)
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