FEATURES

DESCRIPTION

Also known as PCCA_HUMAN, PCCA. This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites (PubMed:8434582, PubMed:6765947). Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA (PubMed:8434582, PubMed:6765947, PubMed:10101253). Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxyl group from carboxylated biotin to propionyl-CoA (By similarity). Propionyl-CoA carboxylase also significantly acts on butyryl-CoA/butanoyl-CoA, which is converted to ethylmalonyl-CoA/(2S)-ethylmalonyl-CoA at a much lower rate (PubMed:6765947). Other alternative minor substrates include (2E)-butenoyl-CoA/crotonoyl-CoA (By similarity). The holoenzyme is a dodecamer composed of 6 PCCA/alpha subunits and 6 PCCB/beta subunits (PubMed:6765947, PubMed:20725044). Interacts (via the biotin carboxylation domain) with SIRT4 (PubMed:23438705). Interacts with SIRT3 and SIRT5 (PubMed:23438705).

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EXTERNAL LINKS

PCCA

Propionyl-CoA carboxylase alpha chain, mitochondrial

ligandability Mutations

PCCA

Molecular Synopsis