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Enzyme Nomenclature
Information on EC 4.1.3.22 - citramalate lyase
for references in articles please use BRENDA:EC4.1.3.22
Word Map on EC 4.1.3.22
- 4.1.3.22
- isoleucine
- jannaschii
-
methanococcus
-
ammonia-lyase
- interrogans
- leptospira
-
isotopomer
- tetanomorphum
- citraconate
- isopropylmalate
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
4.1.3.22
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RECOMMENDED NAME
GeneOntology No.
citramalate lyase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2S)-2-hydroxy-2-methylbutanedioate = acetate + pyruvate
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-
-
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(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
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
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-
-
acetate + pyruvate
(+)-citramalate
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enzyme of the citramalate cycle, acetate assimilation involves the operation of the citramalate cycle
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-
?
acetate + pyruvate
citramalate
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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
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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
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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
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-
-
?
citramalate
acetate + pyruvate
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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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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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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INHIBITORS
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
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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
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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
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pH 6.0: 52% of maximal activity, pH 8.0: 77% of maximal activity, in 50 mM potassium phosphate buffer
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
520000 - 580000
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gel filtration, sucrose density gradient centrifugation
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
oligomer
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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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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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ENGINEERING
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
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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
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DLCR7 (tdcB::Kn cimA::Gm)
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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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LINKS TO OTHER DATABASES (specific for EC-Number 4.1.3.22)
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