Methylmalonyl-CoA carboxytransferase
| methylmalonyl-CoA carboxytransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Methylmalonyl-CoA carboxytransferase homohexamer, Propionibacterium | |||||||||
| Identifiers | |||||||||
| EC no. | 2.1.3.1 | ||||||||
| CAS no. | 9029-86-1 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| 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
The enzyme can convert pyruvate to oxaloacetate, using (S)-methylmalonyl-CoA as its cofactor.[1][2][3]
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 PDB: 1DCZ, PDB: 1DD2, PDB: 1ON3, PDB: 1ON9, PDB: 1RQB, PDB: 1RQE, PDB: 1RQH, PDB: 1RR2, PDB: 1S3H, PDB: 1U5J, PDB: 2D5D, and PDB: 2EVB.
References
- ↑ Enzyme 2.1.3.1 at KEGG Pathway Database.
- ↑ 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.