The enzyme 2,3-dimethylmalate lyase (EC 4.1.3.32) catalyzes the chemical reaction
| 2,3-dimethylmalate lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.3.32 | ||||||||
| CAS no. | 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 / QuickGO | ||||||||
| |||||||||
- (2R,3S)-2,3-dimethylmalate propanoate + 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.
- Pirzer P, Lill U, Eggerer H (1979). “Nicotinic acid metabolism. 2,3-Dimethylmalate lyase”. Hoppe-Seyler’s 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. Bibcode:2006PNAS..10312341A. doi:10.1073/pnas.0601635103. PMC 1562527. PMID 16894175.
