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Information on EC 2.3.3.21 - (R)-citramalate synthase
for references in articles please use BRENDA:EC2.3.3.21
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.3 Acyl groups converted into alkyl groups on transfer
2.3.3.21 (R)-citramalate synthase
IUBMB Comments
One of the enzymes involved in a pyruvate-derived pathway for isoleucine biosynthesis that is found in some bacterial and archaeal species [1,2]. The enzyme can be inhibited by isoleucine, the end-product of the pathway, but not by leucine . The enzyme is highly specific for pyruvate as substrate, as the 2-oxo acids 3-methyl-2-oxobutanoate, 2-oxobutanoate, 4-methyl-2-oxopentanoate, 2-oxohexanoate and 2-oxoglutarate cannot act as substrate [1,2].
The expected taxonomic range for this enzyme is: Bacteria, Archaea
- 2.3.3.21
- synthesis
- acetyl-coa
- isoleucine
-
leptospira
- propionyl-coa
-
interrogans
-
beta-strands
- medicine
-
propionicum
- 2-hydroxybutyrate
-
pane
- polyhydroxyalkanoates
-
leptospirosis
-
phaab
- biotechnology
- energy production
- biofuel production
showSynonyms
licms, licmsc, cima3.7, (r)-citramalate synthase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CimA
citramalate lyase
citramalate synthase
EC 2.3.1.182
-
-
formerly
-
citramalate synthase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + pyruvate + H2O = CoA + (2R)-2-hydroxy-2-methylbutanedioate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
condensation
elimination
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
L-isoleucine biosynthesis II
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + pyruvate
(3S)-citramalyl-CoA
-
Substrates: the enzyme is strictly specific for pyruvate as keto acid substrate
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + (2S)-2-hydroxy-2-methylbutanedioate
Substrates: -
Products: -
Products: -
r
pyruvate + acetyl-CoA + H2O
(2R)-2-hydroxy-2-methylbutanedioate + CoA
Substrates: -
Products: -
Products: -
?
(2S)-2-hydroxy-2-methylbutanedioate
acetate + pyruvate
-
Substrates: -
Products: -
Products: -
?
(2S)-2-hydroxy-2-methylbutanedioate
acetate + pyruvate
-
Substrates: -
Products: -
Products: -
r
(2S)-2-hydroxy-2-methylbutanedioate
acetate + pyruvate
-
Substrates: -
Products: -
Products: -
?
(2S)-2-hydroxy-2-methylbutanedioate
acetate + pyruvate
-
Substrates: -
Products: -
Products: -
r
(2S)-2-hydroxy-2-methylbutanedioate
acetate + pyruvate
-
Substrates: -
Products: -
Products: -
r
acetate + pyruvate
citramalate
Substrates: -
Products: -
Products: -
?
acetate + pyruvate
citramalate
Substrates: -
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
(2S)-2-hydroxy-2-methylbutanedioate + CoA
-
Substrates: -
Products: -
Products: -
r
acetyl-CoA + pyruvate + H2O
(2S)-2-hydroxy-2-methylbutanedioate + CoA
-
Substrates: -
Products: -
Products: -
r
acetyl-CoA + pyruvate + H2O
(2S)-2-hydroxy-2-methylbutanedioate + CoA
-
Substrates: -
Products: -
Products: -
r
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methyl-butanedioate
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methyl-butanedioate
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
-
Substrates: -
Products: i.e. (-)-citramalate
Products: i.e. (-)-citramalate
?
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
-
Substrates: 13C-labeled sodium acetate in culture medium to trace carbon pathways
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
-
Substrates: -
Products: (R)-citramalate is 2-methylmalate
Products: (R)-citramalate is 2-methylmalate
?
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
-
Substrates: the enzyme is involved in the biosynthesis of isoleucine
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
-
Substrates: 14C-labeled acetyl-CoA
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + (R)-citramalate
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + (R)-citramalate
-
Substrates: the enzyme is involved in the threonine-independent biosynthesis of isoleucine via an alternative beta-methyl-D-malate pathway, the expression of cimA is transcriptionally regulated by isoleucine
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + (R)-citramalate
-
Substrates: the enzyme is strictly specific for pyruvate as the keto acid substrate
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + (R)-citramalate
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + (R)-citramalate
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + (R)-citramalate
Substrates: the organism exhibits an inactive pentose phosphate pathway and an alternate isoleucine biosynthesis pathway via the citramalate pathway that uses pyruvate and acetyl-CoA as precursors
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + citramalate
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + citramalate
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + citramalate
Substrates: -
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + citramalate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: LA2350 is a citramalate synthase without detectable alpha-isopropylmalate synthase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: LiCMS shows high substrate specificity for pyruvate, but has very weak or no detectable activities for other alpha-oxo acids, such as glyoxylate, 2-oxobutyrate, and 2-oxoisovalerate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with alpha-ketoglutarate, alpha-ketoadipate, alpha-ketopimelate, alpha-ketoisovalerate, and acetyl-CoA
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + pyruvate + H2O
CoA + (2S)-2-hydroxy-2-methylbutanedioate
Substrates: -
Products: -
Products: -
r
pyruvate + acetyl-CoA + H2O
(2R)-2-hydroxy-2-methylbutanedioate + CoA
Substrates: -
Products: -
Products: -
?
(2S)-2-hydroxy-2-methylbutanedioate
acetate + pyruvate
-
Substrates: -
Products: -
Products: -
?
(2S)-2-hydroxy-2-methylbutanedioate
acetate + pyruvate
-
Substrates: -
Products: -
Products: -
r
(2S)-2-hydroxy-2-methylbutanedioate
acetate + pyruvate
-
Substrates: -
Products: -
Products: -
?
(2S)-2-hydroxy-2-methylbutanedioate
acetate + pyruvate
-
Substrates: -
Products: -
Products: -
r
(2S)-2-hydroxy-2-methylbutanedioate
acetate + pyruvate
-
Substrates: -
Products: -
Products: -
r
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
-
Substrates: 13C-labeled sodium acetate in culture medium to trace carbon pathways
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
-
Substrates: the enzyme is involved in the biosynthesis of isoleucine
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
-
Substrates: 14C-labeled acetyl-CoA
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + (R)-citramalate
-
Substrates: the enzyme is involved in the threonine-independent biosynthesis of isoleucine via an alternative beta-methyl-D-malate pathway, the expression of cimA is transcriptionally regulated by isoleucine
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + (R)-citramalate
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + citramalate
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + citramalate
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + citramalate
Substrates: -
Products: -
Products: -
?
acetyl-CoA + pyruvate + H2O
CoA + citramalate
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Cu2+
-
enzymatic activity of LiCMS in the absence and presence of different metal ions. Cu2+ is an inhibitor
K+
Mg2+
Mn2+
NH4+
Ni2+
Zn2+
Ca2+
-
enzymatic activity of LiCMS in the absence and presence of different metal ions. Ca2+ is an activator
Co2+
-
enzymatic activity of LiCMS in the absence and presence of different metal ions. Co2+ is an activator
K+
-
enzymatic activity of LiCMS in the absence and presence of different metal ions. Co-activation by K+ in the presence of Mn2+
Mg2+
-
enzymatic activity of LiCMS in the absence and presence of different metal ions. Mg2+ is an activator
Mn2+
-
enzymatic activity of LiCMS in the absence and presence of different metal ions. Enzyme shows the highest activity in the presence of Mn2+. Coactivation by K+
Ni2+
-
enzymatic activity of LiCMS in the absence and presence of different metal ions. Ni2+ is an activator
Zn2+
-
enzymatic activity of LiCMS in the absence and presence of different metal ions. Zn2+ is an inhibitor
Zn2+
-
bound, responsible for tetramer formation, removal or mutation of the binding sites by replacement of the histidine 400 and 408 by alanine leads to dimer formation
Zn2+
-
type II crystal structure contains two Zn2+ ions (which are located on the 2fold symmetry axis with an occupancy of 0.5) in the asymmetric unit. The type III crystal structure contains one Zn2+ ion in the asymmetric unit
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
mutant I458A is not inhibited by isoleucine, leucine does not inhibit the wild-type and the mutants H400A/H408A, Y430L, L451V, I458A, D431A, T464A, P493A, and Q495A
-
isoleucine
-
end product feedback inhibition, competitive inhibition of the binding of pyruvate and acetyl-CoA; inhibits in a concentration-dependent manner. High selectivity of CMS for isoleucine over leucine is primarily dictated by the residues, Tyr430, Leu451, Tyr454, Ile458 and Val468, that form a hydrophobic pocket to accommodate the side chain of the inhibitor. Binding of isoleucine affects the binding of the substrate and coenzyme at the active site, possibly via conformational change of the dimer interface of the regulatory domain, leading to inhibition of the catalytic reaction, in a typical pattern of K-type inhibition
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.626
acetyl-CoA
-
mutant T464A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.626
acetyl-CoA
-
T464A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
0.629
acetyl-CoA
-
D431A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
0.629
acetyl-CoA
-
mutant D431A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.712
acetyl-CoA
-
mutant Q495A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.712
acetyl-CoA
-
Q495A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
0.743
acetyl-CoA
-
mutant P493A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.743
acetyl-CoA
-
P493A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
0.803
acetyl-CoA
-
mutant Y454A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.803
acetyl-CoA
-
Y454A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
0.838
acetyl-CoA
-
I458A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
0.838
acetyl-CoA
-
mutant I458A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
1.097
acetyl-CoA
-
mutant Y430L, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
1.097
acetyl-CoA
-
Y430L 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
1.116
acetyl-CoA
-
mutant V468A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
1.116
acetyl-CoA
-
V468A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
1.118
acetyl-CoA
-
wild type, kinetic data for the C-terminal region of LiCMS
1.118
acetyl-CoA
-
wild type, kinetic data for the catalytic reaction of the active site of LiCMS
1.118
acetyl-CoA
-
wild type, kinetic data for the substrate-binding site of LiCMS
1.118
acetyl-CoA
-
wild-type, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
1.118
acetyl-CoA
-
wild-type, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
1.137
acetyl-CoA
-
mutant L81A, kinetic data for the substrate-binding site of LiCMS
1.214
acetyl-CoA
-
mutant L81V, kinetic data for the substrate-binding site of LiCMS
1.511
acetyl-CoA
-
mutant E146D, kinetic data for the catalytic reaction of the active site of LiCMS
1.554
acetyl-CoA
-
H400A/H408A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
1.554
acetyl-CoA
-
mutant H400A/H408A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
1.691
acetyl-CoA
-
mutant Y144V, kinetic data for the substrate-binding site of LiCMS
1.711
acetyl-CoA
-
L451V 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
1.711
acetyl-CoA
-
mutant L451V, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
1.904
acetyl-CoA
-
mutant Y144L, kinetic data for the substrate-binding site of LiCMS
2.272
acetyl-CoA
-
wild-type, 20 microM isoleucine, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
2.272
acetyl-CoA
-
wild-type, in the presence of 0.02 mM isoleucine, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
2.391
acetyl-CoA
-
mutant E146Q, kinetic data for the catalytic reaction of the active site of LiCMS
2.409
acetyl-CoA
-
mutant N310A, kinetic data for the C-terminal region of LiCMS
3.028
acetyl-CoA
-
mutant L104V, kinetic data for the substrate-binding site of LiCMS
4.246
acetyl-CoA
-
wild-type, 60 microM isoleucine, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
4.246
acetyl-CoA
-
wild-type, in the presence of 0.06 mM isoleucine, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
5.186
acetyl-CoA
-
mutant F83A, kinetic data for the catalytic reaction of the active site of LiCMS
5.273
acetyl-CoA
-
LiCMSN, kinetic data for the catalytic reaction of the active site of LiCMS
5.851
acetyl-CoA
-
mutant D304A, kinetic data for the C-terminal region of LiCMS
8.921
acetyl-CoA
-
mutant L311A, kinetic data for the C-terminal region of LiCMS
0.06
pyruvate
-
wild type, kinetic data for the C-terminal region of LiCMS
0.06
pyruvate
-
wild type, kinetic data for the catalytic reaction of the active site of LiCMS
0.06
pyruvate
-
wild type, kinetic data for the substrate-binding site of LiCMS
0.06
pyruvate
-
wild-type, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
0.06
pyruvate
-
wild-type, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.094
pyruvate
-
wild-type, 1 microM isoleucine, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
0.094
pyruvate
-
wild-type, in the presence of 0.001 mM isoleucine, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.105
pyruvate
-
mutant L104V, kinetic data for the substrate-binding site of LiCMS
0.15
pyruvate
-
LiCMSN, kinetic data for the catalytic reaction of the active site of LiCMS
0.153
pyruvate
-
mutant D304A, kinetic data for the C-terminal region of LiCMS
0.17
pyruvate
-
mutant N310A, kinetic data for the C-terminal region of LiCMS
0.178
pyruvate
-
wild-type, 4 microM isoleucine, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
0.178
pyruvate
-
wild-type, in the presence of 0.004 mM isoleucine, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.198
pyruvate
-
mutant L81V, kinetic data for the substrate-binding site of LiCMS
0.263
pyruvate
-
mutant D17N, kinetic data for the catalytic reaction of the active site of LiCMS
0.282
pyruvate
-
mutant L81A, kinetic data for the substrate-binding site of LiCMS
0.979
pyruvate
-
mutant T179A, kinetic data for the catalytic reaction of the active site of LiCMS
1.272
pyruvate
-
mutant L311A, kinetic data for the C-terminal region of LiCMS
2.036
pyruvate
-
mutant D17A, kinetic data for the catalytic reaction of the active site of LiCMS
6.859
pyruvate
-
mutant Y144V, kinetic data for the substrate-binding site of LiCMS
15.53
pyruvate
-
mutant Y144L, kinetic data for the substrate-binding site of LiCMS
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE