Information on EC 4.1.3.25 - (S)-citramalyl-CoA lyase

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

EC NUMBER
COMMENTARY hide
4.1.3.25
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RECOMMENDED NAME
GeneOntology No.
(S)-citramalyl-CoA lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(3S)-citramalyl-CoA = acetyl-CoA + pyruvate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
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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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Carbon fixation pathways in prokaryotes
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glyoxylate assimilation
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itaconate degradation
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Metabolic pathways
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
(3S)-citramalyl-CoA pyruvate-lyase (acetyl-CoA-forming)
Requires Mg2+ ions for activity [3]. The enzyme from the bacterium Clostridium tetanomorphum is a component of EC 4.1.3.22, citramalate lyase [2]. It also acts on (3S)-citramalyl thioacyl-carrier protein [2]. The enzyme from the bacterium Chloroflexus aurantiacus also has the activity of EC 4.1.3.24, malyl-CoA lyase [3]. It has no activity with (3R)-citramalyl-CoA (cf. EC 4.1.3.46, (R)-citramalyl-CoA lyase) [3].
CAS REGISTRY NUMBER
COMMENTARY hide
37290-68-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
gene ccl or PA0883
UniProt
Manually annotated by BRENDA team
NCIB9869
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Manually annotated by BRENDA team
NCIB9869
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Manually annotated by BRENDA team
strain B2aba
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Manually annotated by BRENDA team
strain B2aba
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Manually annotated by BRENDA team
respiration-deficient mutant
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Manually annotated by BRENDA team
gene ccl or Y2383 or ripC
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
additional information
upon ligand binding, changes in the C-terminal domains of the enzyme results in closing of the active site, with the C-terminal domain of one monomer forming a lid over and contributing side chains to the active site of the adjacent monomer, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3S)-citramalyl-CoA
acetyl-CoA + pyruvate
show the reaction diagram
(3S)-citramalyl-thio-acylcarrier protein
?
show the reaction diagram
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?
(S)-citramalyl-CoA
acetyl-CoA + pyruvate
show the reaction diagram
acetyl-CoA + pyruvate
(3S)-citramalyl-CoA
show the reaction diagram
additional information
?
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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
(S)-citramalyl-CoA
acetyl-CoA + pyruvate
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dehospho-CoA
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EC 4.1.3.22 and EC 4.1.3.25 have a common prosthetic group, which is covalently-bound dephospho-CoA. The linkage between dephospho-CoAs and the protein occurs through ribose-5-phosphate. This is bound in phosphodiester linkage to Ser and glycosidically to the 2'- or 3'-hydroxyl group of ribose of dephospho-CoA
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38400
6 * 38400, about, sequence calculation, dimer of trimers, elaborations on the canonical beta8/alpha8 TIM barrel fold and form hexameric assemblies. The trimeric assembly itself is a prerequisite for the catalytic activity
228000
recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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MW of beta-subunit is 33000-36000 Da, EC 4.1.3.25 is the beta-subunit of the enzyme complex EC 4.1.3.22, that has the structure(alpha,beta,gamma)6, SDS-PAGE
hexamer
additional information
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EC 4.1.3.25 is the beta-subunit of EC 4.1.3.22
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, alone or in complex with substrate propionyl-CoA, inhibitor oxalate, and magnesium ions, pH 5.5, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement modeling
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
copurification of citramate cleavage enzymes EC 4.2.3.25 and EC 4.2.1.22
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recombinant enzyme from Escherichia coli
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 cells
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gene ccl or PA0883 , genetic structure, the enzyme is encoded in a six-gene operon
gene ccl or Y2383 or ripC, genetic structure, the enzyme is encoded in a three-gene operon, in vitro reconstitution of itaconate degradation pathway with the heterologously produced and purified enzymes from Yersinia pestis
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phylogenetic analysis, recombinant expression in Escherichia coli