2,3-dimethylmalate lyase
2,3-dimethylmalate lyase | |||||||||
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Identifiers | |||||||||
EC number | 4.1.3.32 | ||||||||
CAS number | 73562-28-4 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / EGO | ||||||||
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In enzymology, a 2,3-dimethylmalate lyase (EC 4.1.3.32) is an enzyme that catalyzes the chemical reaction
- (2R,3S)-2,3-dimethylmalate propanoate + pyruvate
Hence, this enzyme has one substrate, (2R,3S)-2,3-dimethylmalate, and two products, propanoate and pyruvate.
This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is (2R,3S)-2,3-dimethylmalate pyruvate-lyase (propanoate-forming). Other names in common use include 2,3-dimethylmalate pyruvate-lyase, and (2R,3S)-2,3-dimethylmalate pyruvate-lyase. This enzyme participates in c5-branched dibasic acid metabolism.
References
- Pirzer P, Lill U, Eggerer H (1979). "Nicotinic acid metabolism. 2,3-Dimethylmalate lyase". Hoppe. Seylers. Z. Physiol. Chem. 360 (12): 1693–702. doi:10.1515/bchm2.1979.360.2.1693. PMID 527937.
- Alhapel A, Darley DJ, Wagener N, Eckel E, Elsner N, Pierik AJ (2006). "Molecular and functional analysis of nicotinate catabolism in Eubacterium barkeri". Proc. Natl. Acad. Sci. U.S.A. 103 (33): 12341–6. doi:10.1073/pnas.0601635103. PMC 1562527. PMID 16894175.
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