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 37°C
37.43
in TES buffer (0.1 M, pH 7.5), at 37°C
39.42
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
80.92
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
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
-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
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