Methylmalonyl-CoA carboxytransferase

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


 * (S)-methylmalonyl-CoA + pyruvate $$\rightleftharpoons$$ 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, , , , , , , , , , , and.