Information on EC - methylmalonyl-CoA carboxytransferase

for references in articles please use BRENDA:EC2.1.3.1
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IUBMB Comments
A biotinyl-protein, containing cobalt and zinc. The enzyme, described from the bacterium Propionibacterium shermanii, is unique among the biotin-dependent enzymes in that it catalyses carboxyl transfer between two organic molecules, utilizing two separate carboxyltransferase domains. The enzyme is a very large complex, consisting of a hexameric central core of 12S subunits surrounded by six 5S subunit dimers, each connected to the central core by twelve 1.3S biotin carrier subunits.
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
5S subunit of transcarboxylase, carboxyltransferase subunit of acetyl-CoA carboxylase, carboxyltransferase, methylmalonyl coenzyme A, DtsR1, MCT, methyl malonyl CoA carboxyl transferase, methylmalonyl CoA carboxyltransferase, methylmalonyl CoA-oxalacetate transcarboxylase, methylmalonyl coenzyme A carboxyltransferase, methylmalonyl-CoA carboxyltransferase, more
(S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate
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