Information on EC 4.1.3.22 - citramalate lyase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
4.1.3.22
-
RECOMMENDED NAME
GeneOntology No.
citramalate lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2S)-2-hydroxy-2-methylbutanedioate = acetate + pyruvate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
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-
-
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elimination
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of an oxo-acid, C-C bond cleavage
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
C5-Branched dibasic acid metabolism
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L-glutamate degradation VI (to pyruvate)
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glutamate and glutamine metabolism
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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).
CAS REGISTRY NUMBER
COMMENTARY hide
9027-93-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain H1
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-
Manually annotated by BRENDA team
ATCC 51573, strain DL1
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-
Manually annotated by BRENDA team
ATCC 51573, strain DL1
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-
Manually annotated by BRENDA team
fragment; serovar Semaranga
SwissProt
Manually annotated by BRENDA team
no activity in Clostridium kluyveri
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-
-
Manually annotated by BRENDA team
no activity in Escherichia coli
ATCC 4157
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-
Manually annotated by BRENDA team
no activity in Pseudomonas sp.
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-
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Manually annotated by BRENDA team
no activity in Saccharomyces cerevisiae
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-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetate + pyruvate
(+)-citramalate
show the reaction diagram
acetate + pyruvate
citramalate
show the reaction diagram
citramalate
2-oxobutanoate + ?
show the reaction diagram
citramalate
acetate + pyruvate
show the reaction diagram
additional information
?
-
-
the enzyme is involved in the fermentation of glutamate
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetate + pyruvate
(+)-citramalate
show the reaction diagram
-
enzyme of the citramalate cycle, acetate assimilation involves the operation of the citramalate cycle
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-
?
acetate + pyruvate
citramalate
show the reaction diagram
additional information
?
-
-
the enzyme is involved in the fermentation of glutamate
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-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
Mn2+, Mg2+ or Co2+ required
Mn2+
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Mn2+, Mg2+ or Co2+ required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dephospho-CoA
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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 hide
LITERATURE
IMAGE
0.6
(+)-citramalate
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0004
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in mutant strain DLCR6 (cimA::Gm); in mutant strain DLCR7 (tdcB::Kn cimA::Gm)
0.0074
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DL1 (wild type)
33.14
in TES buffer (0.1 M, pH 7.5), at 37C
37.43
in TES buffer (0.1 M, pH 7.5), at 37C
39.42
in TES buffer (0.1 M, pH 7.5), at 37C
44.35
in TES buffer (0.1 M, pH 7.5), at 37C
51.29
in TES buffer (0.1 M, pH 7.5), at 37C
53.68
in TES buffer (0.1 M, pH 7.5), at 37C
64.75
in TES buffer (0.1 M, pH 7.5), at 37C
76.46
in TES buffer (0.1 M, pH 7.5), at 37C
80.92
in TES buffer (0.1 M, pH 7.5), at 37C
82.36
in TES buffer (0.1 M, pH 7.5), at 37C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3 - 7.5
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50 mM potassium phosphate buffer
8 - 8.2
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Tris-HCl buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
520000 - 580000
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gel filtration, sucrose density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DLCR6 (cimA::Gm)
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citramalate synthase knockout mutant
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
DLCR6 (cimA::Gm)
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citramalate synthase knockout mutant
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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
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DLCR6 (cimA::Gm)
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citramalate synthase knockout mutant
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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
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additional information