Methylmalonyl-CoA carboxytransferase
| methylmalonyl-CoA carboxytransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Methylmalonyl-CoA carboxytransferase homohexamer, Propionibacterium | |||||||||
| Identifiers | |||||||||
| EC no. | 2.1.3.1 | ||||||||
| CAS no. | 9029-86-1 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a methylmalonyl-CoA carboxytransferase (EC 2.1.3.1) is an enzyme that catalyzes the chemical reaction
- (S)-methylmalonyl-CoA + pyruvate propanoyl-CoA + oxaloacetate
Thus, the two substrates of this enzyme are (S)-methylmalonyl-CoA and pyruvate, whereas its two products are propanoyl-CoA and oxaloacetate.
This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the carboxy- and carbamoyltransferases. The systematic name of this enzyme class is (S)-methylmalonyl-CoA:pyruvate carboxytransferase. Other names in common use include transcarboxylase, methylmalonyl coenzyme A carboxyltransferase, methylmalonyl-CoA transcarboxylase, oxalacetic transcarboxylase, methylmalonyl-CoA carboxyltransferase, methylmalonyl-CoA carboxyltransferase, (S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxyltransferase, (S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxytransferase, and carboxytransferase [incorrect]. This enzyme participates in propanoate metabolism. It has 3 cofactors: zinc, Biotin, and Cobalt.
Structural studies
[edit]As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1DCZ, 1DD2, 1ON3, 1ON9, 1RQB, 1RQE, 1RQH, 1RR2, 1S3H, 1U5J, 2D5D, and 2EVB.
References
[edit]- Hoffmann A, Hilpert W, Dimroth P (1989). "The carboxyltransferase activity of the sodium-ion-translocating methylmalonyl-CoA decarboxylase of Veillonella alcalescens". Eur. J. Biochem. 179 (3): 645–50. doi:10.1111/j.1432-1033.1989.tb14596.x. PMID 2920730.
- Swick RW; Wood HG (1960). "The role of transcarboxylation in propionic acid fermentation". Proc. Natl. Acad. Sci. USA. 46 (1): 28–41. Bibcode:1960PNAS...46...28S. doi:10.1073/pnas.46.1.28. PMC 285006. PMID 16590594.
