Recombinant Human PCCA protein (GST tag N-Terminus)
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Recombinant Human PCCA protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 703 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
PCCase subunit alpha, Propanoyl-CoA:carbon dioxide ligase subunit alpha, PCCA
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human PCCA protein (GST tag N-Terminus) (AB159059)
ab159059 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Complementary Products
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
PCCA is a part of the propionyl-CoA carboxylase complex which functions as a heterododecameric complex involving both alpha and beta subunits. This enzyme plays an important role in energy metabolism facilitating the conversion of propionyl-CoA into more useful forms for cellular processes. The proper functioning of this complex ensures the breakdown and assimilation of important metabolites aiding in the elimination of toxic intermediates produced during the metabolism of branched-chain amino acids as well as odd-chain fatty acids.
Pathways
The catabolism facilitated by PCCA involves the metabolic pathways of branched-chain amino acids and odd-numbered fatty acids. It fits within the larger methylmalonyl-CoA mutase pathway where it transforms its substrate into an immediate precursor for succinyl-CoA production. The activity in this pathway links PCCA to other proteins such as methylmalonyl-CoA mutase which subsequently acts to convert methylmalonyl-CoA to succinyl-CoA a critical step for entry into the tricarboxylic acid (TCA) cycle.
Specifications
Form
Liquid
General info
Function
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 : 6765947, PubMed : 8434582). Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA (PubMed : 10101253, PubMed : 6765947, PubMed : 8434582). 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).
Post-translational modifications
Acetylated.. The biotin cofactor is covalently attached to the C-terminal biotinyl-binding domain and is required for the catalytic activity (PubMed:10329019). Biotinylation is catalyzed by HLCS (PubMed:20443544, PubMed:7753853).
Subcellular localisation
Mitochondrion matrix
Target data
Product promise
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