Biology:Methylmalonyl-CoA carboxytransferase
| methylmalonyl-CoA carboxytransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Methylmalonyl-CoA carboxytransferase homohexamer, Propionibacterium | |||||||||
| Identifiers | |||||||||
| EC number | 2.1.3.1 | ||||||||
| CAS number | 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 [math]\displaystyle{ \rightleftharpoons }[/math] 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
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
- "The carboxyltransferase activity of the sodium-ion-translocating methylmalonyl-CoA decarboxylase of Veillonella alcalescens". Eur. J. Biochem. 179 (3): 645–50. 1989. 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. doi:10.1073/pnas.46.1.28. PMID 16590594. Bibcode: 1960PNAS...46...28S.
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