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acetyl-CoA + H2O + 2-oxoglutarate
(2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
-
-
?
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
acetyl-CoA + H2O + oxaloacetate
? + CoA
-
oxaloacetate is a substrate with lower affinity than 2-oxoglutarate
-
-
?
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
-
-
?
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
-
-
?
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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
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
-
-
?
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1,10-phenanthroline
-
0.01 mM, 91% inhibition
2,2'-dipyridyl
-
0.01 mM, 82% inhibition
CoA
-
noncompetitive versus acetyl-CoA
Cu2+
-
0.0001 mM CuSO4, complete inhibition
desulfo-CoA
-
uncompetitive
glyoxylate
-
competitive, analysis of pH-dependence of inhibition
Hg2+
-
0.01 mM HgCl2, complete inhibition
iodoacetic acid
-
0.01 mM, 71% inhibition
L-lysine
-
isoform Lys20 is one order of magnitude less sensitive to L-lysine inhibition than Lys21
lysine
strong allosteric inhibitor of Lys21p. Induces positive cooperativity for alpha-ketoglutarate binding
Na2HAsO4
-
0.01 mM, 67% inhibition
NaF
-
0.01 mM, 73% inhibition
p-hydroxymercuribenzoate
-
0.0001 mM, complete inhibition
pyridine-2,3-dicarboxylate
-
-
Pyridine-2,4-dicarboxylate
-
-
Pyridine-2,5-dicarboxylate
-
-
pyridine-2,6-dicarboxylate
-
-
pyridine-2-carboxylate
-
-
thialysine
-
5 mM, complete inhibition
citrate
-
noncompetitive
citrate
-
competitive versus 2-oxoglutarate
hydroxylysine
-
20 mM, 69% inhibition
hydroxylysine
-
DL-hydroxylysine
L-Lys
-
20 mM, 95% inhibition
L-Lys
-
feedback inhibition of homocitrate synthase by lysine modulates the activation of LYS gene expression by transcriptional activator Lys14p
L-Lys
-
10 mM, 80% inhibition. No inhibition by 10 mM D-Lys
Lys
-
binding to the less active enzyme conformer
Lys
-
feedback inhibitor, competitive versus 2-oxoglutarate and linear in the physiological range of lysine concentrations up to 5 mM
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
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26
2-oxoglutarate
-
pH 7.2
10
2-Oxomalonate
-
pH 7.2
7.7
oxalylglycine
-
pH 7.2
3
pyridine-2,3-dicarboxylate
-
pH 7.2
0.6
Pyridine-2,4-dicarboxylate
-
pH 7.2
14
Pyridine-2,5-dicarboxylate
-
pH 7.2
0.7
pyridine-2,6-dicarboxylate
-
pH 7.2
0.43
pyridine-2-carboxylate
-
pH 7.2
46
succinyl phosphonate
-
pH 7.2
additional information
additional information
-
-
-
13.5
citrate
-
Kis, varied substrate is 2-oxoglutarate, fixed substrate: 0.031 mM acetyl-CoA
19
citrate
-
Kis, varied substrate is acetyl-CoA, fixed substrate: 5 mM 2-oxoglutarate
200
citrate
-
Kii, varied substrate is acetyl-CoA, fixed substrate: 5 mM 2-oxoglutarate
0.008
CoA
-
Kis, varied substrate acetyl-CoA, fixed substrate: 5 mM 2-oxoglutarate
0.024
CoA
-
Kii, varied substrate 2-oxoglutarate, fixed substrate: 0.031 mM acetyl-CoA
0.033
CoA
-
Kii, varied substrate acetyl-CoA, fixed substrate: 5 mM 2-oxoglutarate
0.014
desulfo-CoA
-
Kis, varied substrate acetyl-CoA, fixed substrate: 5 mM 2-oxoglutarate
0.021
desulfo-CoA
-
Kii, varied substrate 2-oxoglutarate, fixed substrate: 0.031 mM acteyl-CoA
0.18
desulfo-CoA
-
Kii, varied substrate acetyl-CoA, fixed substrate: 5 mM 2-oxoglutarate
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Strassman, M.; Ceci, L.N.
Enzymatic formation of homocitric acid, an intermediate in lysine biosynthesis
Biochem. Biophys. Res. Commun.
14
262-267
1964
Saccharomyces cerevisiae
brenda
Tucci, A.F.; Ceci, L.N.
Homocitrate synthase from yeast
Arch. Biochem. Biophys.
153
742-750
1972
Saccharomyces cerevisiae
brenda
Gray, G.S.; Bhattacharjee, J.K.
Biosynthesis of lysine in Saccharomyces cerevisiae: properties and spectrophotometric determination of homocitrate synthase activity
Can. J. Microbiol.
22
1664-1667
1976
Saccharomyces cerevisiae
brenda
Gray, G.S.; Bhattacharjee, J.K.
Biosynthesis of lysine in Saccharomyces cerevisiae: Regulation of homocitrate synthase in analogue-resistant mutants
J. Gen. Microbiol.
97
117-120
1976
Saccharomyces cerevisiae
brenda
Ramos, F.; Verhasselt, P.; Fellers, A.; Peeters, P.; Wach, A.; Dubois, E.; Volckaert, G.
Identification of the gene encoding a homocitrate synthase isoenzyme of Saccharomyces cerevisiae
Yeast
12
1315-1320
1996
Saccharomyces cerevisiae
brenda
Chen, S.; Brockenbrough, J.S.; Dove, J.E.; Aris, P.
Homocitrate synthase is located in the nucleus in the yeast Saccharomyces cerevisiae
J. Biol. Chem.
272
10839-10846
1997
Saccharomyces cerevisiae
brenda
Feller, A.; Ramos, F.; Pierard, A.; Dubois, E.
In Saccharomyces cerevisiae, feedback inhibition of homocitrate synthase by lysine modulates the activation of LYS gene expression by Lys14p
Eur. J. Biochem.
261
163-170
1999
Saccharomyces cerevisiae
brenda
Banuelos, O.; Casqueiro, J.; Steidl, S.; Gutierrez, S.; Brakhage, A.; Martin, J.F.
Subcellular localization of the homocitrate synthase in Penicillium chrysogenum
Mol. Gen. Genet.
266
711-719
2002
Saccharomyces cerevisiae, Penicillium chrysogenum
brenda
Andi, B.; West, A.H.; Cook, P.F.
Stabilization and characterization of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae
Arch. Biochem. Biophys.
421
243-254
2004
Saccharomyces cerevisiae
brenda
Andi, B.; West, A.H.; Cook, P.F.
Kinetic mechanism of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae
Biochemistry
43
11790-11795
2004
Saccharomyces cerevisiae
brenda
Andi, B.; West, A.H.; Cook, P.F.
Regulatory mechanism of Histidine-tagged homocitrate synthase from Saccharomyces cerevisiae: I. KINETIC STUDIES
J. Biol. Chem.
280
31624-31632
2005
Saccharomyces cerevisiae
brenda
Andi, B.; Cook, P.F.
Regulatory mechanism of Histidine-tagged homocitrate synthase from Saccharomyces cerevisiae: II. THEORY
J. Biol. Chem.
280
31633-31640
2005
Saccharomyces cerevisiae
brenda
Qian, J.; West, A.H.; Cook, P.F.
Acid-base chemical mechanism of homocitrate synthase from Saccharomyces cerevisiae
Biochemistry
45
12136-12143
2006
Saccharomyces cerevisiae
brenda
Qian, J.; Khandogin, J.; West, A.H.; Cook, P.F.
Evidence for a catalytic dyad in the active site of homocitrate synthase from Saccharomyces cerevisiae
Biochemistry
47
6851-6858
2008
Saccharomyces cerevisiae
brenda
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
Microbiology
154
1656-1667
2008
Saccharomyces cerevisiae (P48570), Saccharomyces cerevisiae (Q12122), Saccharomyces cerevisiae
brenda
Scott, E.M.; Pillus, L.
Homocitrate synthase connects amino acid metabolism to chromatin functions through Esa1 and DNA damage
Genes Dev.
24
1903-1913
2010
Saccharomyces cerevisiae
brenda
Quezada, H.; Marin-Hernandez, A.; Aguilar, D.; Lopez, G.; Gallardo-Perez, J.C.; Jasso-Chavez, R.; Gonzalez, A.; Saavedra, E.; Moreno-Sanchez, R.
The Lys20 homocitrate synthase isoform exerts most of the flux control over the lysine synthesis pathway in Saccharomyces cerevisiae
Mol. Microbiol.
82
578-590
2011
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
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.
6
1922-1930
2017
Saccharomyces cerevisiae (P48570), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P48570)
brenda