PCCA : propionyl-CoA carboxylase subunit alpha
Description
The PCCA (propionyl-CoA carboxylase subunit alpha) is a protein-coding gene located on chromosome 13.
The PCCA gene provides instructions for making a part of the propionyl-CoA carboxylase enzyme, specifically the alpha subunit. This enzyme is made up of six alpha subunits and six beta subunits (produced by the PCCB gene). The alpha subunit also binds to the B vitamin biotin. Propionyl-CoA carboxylase is involved in the normal processing of proteins. It breaks down the amino acids isoleucine, methionine, threonine, and valine, and also helps break down certain types of lipids (fats) and cholesterol. These molecules are first converted to propionyl-CoA, which is then converted to methylmalonyl-CoA by propionyl-CoA carboxylase using biotin. Additional enzymes then break down methylmalonyl-CoA into other molecules used for energy.
The PCCA gene encodes the alpha subunit of propionyl-CoA carboxylase (PCC), a mitochondrial enzyme crucial for the breakdown of specific amino acids (isoleucine, methionine, threonine, valine), odd-chain fatty acids, and certain metabolites. PCC catalyzes the carboxylation of propionyl-CoA to D-methylmalonyl-CoA. This process involves the alpha subunit catalyzing the ATP-dependent carboxylation of biotin carried by the biotin carboxyl carrier (BCC) domain. Subsequently, the beta subunit transfers the carboxyl group from carboxylated biotin to propionyl-CoA. PCC also demonstrates significant activity towards butyryl-CoA, converting it to ethylmalonyl-CoA at a lower rate. Minor substrates include crotonoyl-CoA. The holoenzyme, a dodecamer, comprises six PCCA/alpha subunits and six PCCB/beta subunits. The alpha subunit interacts with SIRT4, SIRT3, and SIRT5 through its biotin carboxylation domain.
PCCA is also known as -.
