Methylmalonyl-CoA carboxytransferase

In enzymology, a methylmalonyl-CoA carboxytransferase (EC 2.1.3.1) is an enzyme that catalyzes the chemical reaction

methylmalonyl-CoA carboxytransferase
Methylmalonyl-CoA carboxytransferase homohexamer, Propionibacterium
Identifiers
EC no.2.1.3.1
CAS no.9029-86-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
(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.