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Information on EC 4.1.3.22 - citramalate lyase
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4.1.3.22 citramalate lyaseIUBMB Comments
The enzyme can be dissociated into components, two of which are identical with EC 2.8.3.11 (citramalate CoA-transferase) and EC 4.1.3.25 (citramalyl-CoA lyase).
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Word Map
- 4.1.3.22
- isoleucine
- jannaschii
-
methanococcus
- interrogans
- leptospira
-
isotopomer
- tetanomorphum
- citraconate
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
(+)-citramalate pyruvate-lyase, (S)-citramalate lyase, CimA, citramalate lyase, citramalate synthase, citramalate synthetase, citramalic synthase, citramalic-condensing enzyme, CMS, GSU1798, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(+)-citramalate pyruvate-lyase
-
-
-
-
(S)-citramalate lyase
-
-
-
-
CimA
citramalate lyase
citramalate synthase
citramalate synthetase
-
-
-
-
citramalic synthase
-
-
-
-
citramalic-condensing enzyme
-
-
-
-
GSU1798
lyase, citramalate
-
-
-
-
citramalate lyase
-
citramalate synthase
-
-
-
-
GSU1798
Geobacter sulfurreducens ATCC 51573 / DSM 12127
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represents a novel phylogenetic variant of the enzyme
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GSU1798
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represents a novel phylogenetic variant of the enzyme
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2S)-2-hydroxy-2-methylbutanedioate = acetate + pyruvate
-
-
-
-
(2S)-2-hydroxy-2-methylbutanedioate = acetate + pyruvate
reversible nucleophilic addition of acetyl thioester to carbonyl groups with inversion of congfiguration
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
condensation
-
-
-
-
elimination
-
-
of an oxo-acid, C-C bond cleavage
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(2S)-2-hydroxy-2-methylbutanedioate pyruvate-lyase (acetate-forming)
The enzyme can be dissociated into components, two of which are identical with EC 2.8.3.11 (citramalate CoA-transferase) and EC 4.1.3.25 (citramalyl-CoA lyase).
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CAS REGISTRY NUMBER
COMMENTARY
9027-93-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the enzyme is involved in the fermentation of glutamate
-
-
-
acetate + pyruvate
(+)-citramalate
-
enzyme of the citramalate cycle, acetate assimilation involves the operation of the citramalate cycle
-
-
?
acetate + pyruvate
citramalate
-
citramalate synthase appears to have a high affinity for pyruvate, with 52.5% +/- 4.9% of the activity remaining when the pyruvate concentration is reduced from 1 mM to 0.1 mM
-
-
?
acetate + pyruvate
citramalate
Geobacter sulfurreducens ATCC 51573 / DSM 12127
-
citramalate synthase appears to have a high affinity for pyruvate, with 52.5% +/- 4.9% of the activity remaining when the pyruvate concentration is reduced from 1 mM to 0.1 mM
-
-
?
acetate + pyruvate
citramalate
-
citramalate synthase appears to have a high affinity for pyruvate, with 52.5% +/- 4.9% of the activity remaining when the pyruvate concentration is reduced from 1 mM to 0.1 mM
-
-
?
acetate + pyruvate
citramalate
-
-
-
?
citramalate
acetate + pyruvate
-
the alpha-subunit catalyzes the formation of acetyl-CoA and citramalate. The beta-subunit catalyzes the cleavage of (3S)-citramalyl-thio-acyl carrier protein lyase
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetate + pyruvate
(+)-citramalate
-
enzyme of the citramalate cycle, acetate assimilation involves the operation of the citramalate cycle
-
-
?
additional information
?
-
-
the enzyme is involved in the fermentation of glutamate
-
-
-
acetate + pyruvate
citramalate
-
citramalate synthase appears to have a high affinity for pyruvate, with 52.5% +/- 4.9% of the activity remaining when the pyruvate concentration is reduced from 1 mM to 0.1 mM
-
-
?
acetate + pyruvate
citramalate
Geobacter sulfurreducens ATCC 51573 / DSM 12127
-
citramalate synthase appears to have a high affinity for pyruvate, with 52.5% +/- 4.9% of the activity remaining when the pyruvate concentration is reduced from 1 mM to 0.1 mM
-
-
?
acetate + pyruvate
citramalate
-
citramalate synthase appears to have a high affinity for pyruvate, with 52.5% +/- 4.9% of the activity remaining when the pyruvate concentration is reduced from 1 mM to 0.1 mM
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
-
Km for MgCl2: 0.1 mM; or an equivalent divalent cation is required
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dephospho-CoA
-
bound in phosphodiester linkage to Ser and glycosidically to the 2' or 3'-hydroxyl group of ribose of dephospho-CoA
additional information
-
the enzyme contains acetyl thioester residues which play the central role in the catalytic mechanism
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0004
-
in mutant strain DLCR6 (cimA::Gm); in mutant strain DLCR7 (tdcB::Kn cimA::Gm)
37.43
in TES buffer (0.1 M, pH 7.5), at 37°C
44.35
in TES buffer (0.1 M, pH 7.5), at 37°C
51.29
in TES buffer (0.1 M, pH 7.5), at 37°C
53.68
in TES buffer (0.1 M, pH 7.5), at 37°C
64.75
in TES buffer (0.1 M, pH 7.5), at 37°C
76.46
in TES buffer (0.1 M, pH 7.5), at 37°C
82.36
in TES buffer (0.1 M, pH 7.5), at 37°C
additional information
additional information
-
enzymatic activity in mutant strain DLCR5 (tdcB::Kn), a threonine ammonia-lyase knockout mutant (EC 4.3.1.19), is 0.0051 micromol/min/mg
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
-
pH 6.0: 52% of maximal activity, pH 8.0: 77% of maximal activity, in 50 mM potassium phosphate buffer
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
-
key enzyme in metabolic pathways for citramalate synthesis
metabolism
-
key enzyme in metabolic pathways for citramalate synthesis
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
CIMA_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
491
0
53493
Swiss-Prot
A0FDI2_LEPIR
431
0
47831
TrEMBL
A0FDJ0_LEPIR
435
0
48159
TrEMBL
A0FDI4_LEPIR
434
0
48195
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
520000 - 580000
-
gel filtration, sucrose density gradient centrifugation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
oligomer
-
6 * 53000-56000, alpha, + 6 * 33000-36000, beta, + 6 * 10000-12000, gamma, SDS-PAGE
oligomer
-
the alpha-subunit represents an acetyl-thio-acyl carrier protein:citramalate acyl carrier protein transferase and the beta-subunit a (3S)-citramalyl-thio-acyl carrier protein lyase
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DLCR7 (tdcB::Kn cimA::Gm)
-
double (ammonia-lyase (EC 4.3.1.19) and citramalate synthase) knockout mutant. DLCR5 (tdcB::Kn) a threonine ammonia-lyase knockout mutant (EC 4.3.1.19) is also constructed
DLCR6 (cimA::Gm)
Geobacter sulfurreducens ATCC 51573 / DSM 12127
-
citramalate synthase knockout mutant
-
DLCR7 (tdcB::Kn cimA::Gm)
Geobacter sulfurreducens ATCC 51573 / DSM 12127
-
double (ammonia-lyase (EC 4.3.1.19) and citramalate synthase) knockout mutant. DLCR5 (tdcB::Kn) a threonine ammonia-lyase knockout mutant (EC 4.3.1.19) is also constructed
-
DLCR7 (tdcB::Kn cimA::Gm)
-
double (ammonia-lyase (EC 4.3.1.19) and citramalate synthase) knockout mutant. DLCR5 (tdcB::Kn) a threonine ammonia-lyase knockout mutant (EC 4.3.1.19) is also constructed
-
additional information
additional information
-
strain DL1 used to construct strains. Construction of mutants via single-step gene replacement. Mutants lacking both enzymes (citramalate synthase and threonine ammonia-lyase) are auxotrophs for isoleucine, whereas single mutants are capable of growth in the absence of isoleucine
additional information
Geobacter sulfurreducens ATCC 51573 / DSM 12127
-
strain DL1 used to construct strains. Construction of mutants via single-step gene replacement. Mutants lacking both enzymes (citramalate synthase and threonine ammonia-lyase) are auxotrophs for isoleucine, whereas single mutants are capable of growth in the absence of isoleucine
-
additional information
-
strain DL1 used to construct strains. Construction of mutants via single-step gene replacement. Mutants lacking both enzymes (citramalate synthase and threonine ammonia-lyase) are auxotrophs for isoleucine, whereas single mutants are capable of growth in the absence of isoleucine
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, enzyme concentration 10 mg/ml, 0.1 M phoshate, pH 7.4, 1.0 mM MgCl2, stable for at least 6 months
-
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
the modified citramalate synthase gene cimA from Methanococcus jannaschii is expressed in Escherichia coli. Gene knockouts and fermentation optimization improve citramalate production from glycerol and also reduce acetate accumulation. Near elimination of acetate formation necessitates deletions in genes for both pathways associated with acetate formation: ackA coding acetate kinase, pta coding phosphotransacetylase, and poxB coding pyruvate oxidase
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
synthesis of citramalic acid from glycerol by metabolically engineered Escherichia coli
synthesis
-
synthesis of citramalate at high yield by Escherichia coli overexpressing citramalate synthase. Citramalate is a chemical precursor to the industrially important methacrylic acid. Acetate is an undesirable by-product potentially formed from pyruvate and acetyl-CoA, the precursors of citramalate during aerobic growth of Escherichia coli. Gene deletions critical to reducing acetate accumulation during aerobic growth and citramalate production are ifdentified in metabolically engineered Escherichia coli strains. The key knockouts critical to minimizing acetate formation are identified as pta, ackA and poxB
synthesis
-
synthesis of citramalate at high yield by Escherichia coli overexpressing citramalate synthase. Citramalate is a chemical precursor to the industrially important methacrylic acid. Acetate is an undesirable by-product potentially formed from pyruvate and acetyl-CoA, the precursors of citramalate during aerobic growth of Escherichia coli. Gene deletions critical to reducing acetate accumulation during aerobic growth and citramalate production are ifdentified in metabolically engineered Escherichia coli strains. The key knockouts critical to minimizing acetate formation are identified as pta, ackA and poxB; synthesis of citramalic acid from glycerol by metabolically engineered Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Barker, H.A.
Citramalate lyase of Clostridium tetanomorphum
Arch. Mikrobiol.
59
4-12
1967
Clostridium tetanomorphum, Clostridium tetanomorphum H1 / ATCC 15920, no activity in Clostridium kluyveri, no activity in Escherichia coli, no activity in Pseudomonas sp., no activity in Saccharomyces cerevisiae
brenda
Barker, H.A.
Citramalate pyruvate lyase
Methods Enzymol.
13
344-346
1969
Clostridium tetanomorphum
-
brenda
Buckel, W.; Bobi, A.
The enzyme complex citramalate lyase from Clostridium tetanomorphum
Eur. J. Biochem.
64
255-262
1976
Clostridium tetanomorphum
brenda
Dimroth, P.; Buckel, W.; Loyal, R.; Eggerer, H.
Isolation and function of the subunits of citramalate lyase and formation of hybrids with the subunits of citrate lyase
Eur. J. Biochem.
80
469-477
1977
Clostridium tetanomorphum
brenda
Dimroth, P.; Loyal, R.
Structure of the prosthetic groups of citrate lyase and citramalate lyase
FEBS Lett.
76
280-283
1977
Clostridium tetanomorphum
brenda
Buckel, W.; Bobi, A.
Substrate stereochemistry of the cleavage reaction in citramalate lyase
Biochem. Soc. Trans.
3
924-926
1975
Clostridium tetanomorphum
-
brenda
Filatova, L.V.; Berg, I.A.; Krasil'nikova, E.N.; Ivanovsky, R.N.
A study of the mechanism of acetate assimilation in purple nonsulfur bacteria lacking the glyoxylate shunt: enzymes of the citramalate cycle in Rhodobacter sphaeroides
Microbiology
74
270-278
2005
Rhodobacter sphaeroides
-
brenda
Zou, Y.; Guo, X.; Picardeau, M.; Xu, H.; Zhao, G.
A comprehensive survey on isoleucine biosynthesis pathways in seven epidemic Leptospira interrogans reference strains of China
FEMS Microbiol. Lett.
269
90-96
2007
Leptospira biflexa (A0FDJ2), Leptospira biflexa (A0FDJ4), Leptospira biflexa, Leptospira interrogans (A0FDH8), Leptospira interrogans (A0FDI0), Leptospira interrogans (A0FDI2), Leptospira interrogans (A0FDI4), Leptospira interrogans (A0FDI6), Leptospira interrogans (A0FDI8), Leptospira interrogans (A0FDJ0), Leptospira interrogans, Leptospira meyeri (A1Z0Z6), Leptospira meyeri
brenda
Drevland, R.M.; Waheed, A.; Graham, D.E.
Enzymology and evolution of the pyruvate pathway to 2-oxobutyrate in Methanocaldococcus jannaschii
J. Bacteriol.
189
4391-4400
2007
Methanocaldococcus jannaschii
brenda
Risso, C.; Van Dien, S.J.; Orloff, A.; Lovley, D.R.; Coppi, M.V.
Elucidation of an alternate isoleucine biosynthesis pathway in Geobacter sulfurreducens
J. Bacteriol.
190
2266-2274
2008
Geobacter sulfurreducens, Geobacter sulfurreducens ATCC 51573 / DSM 12127
brenda
Wu, X.; Eiteman, M.A.
Synthesis of citramalic acid from glycerol by metabolically engineered Escherichia coli
J. Ind. Microbiol. Biotechnol.
44
1483-1490
2017
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii (Q58787), Methanocaldococcus jannaschii DSM 2661 (Q58787)
brenda
Parimi, N.S.; Durie, I.A.; Wu, X.; Niyas, A.M.M.; Eiteman, M.A.
Eliminating acetate formation improves citramalate production by metabolically engineered Escherichia coli
Microb. Cell Fact.
16
114
2017
Methanocaldococcus jannaschii (Q58787), Methanocaldococcus jannaschii DSM 2661 (Q58787)
brenda
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