Branched-chain amino acid aminotransferase
| Branched-chain amino acid aminotransferase | |||||||
|---|---|---|---|---|---|---|---|
Crystallographic structure of branched-chain-amino-acid aminotransferase from Mycobacterium smegmatis | |||||||
| Identifiers | |||||||
| Symbol | BCAT | ||||||
| Alt. symbols | BCT | ||||||
| NCBI gene | 587 | ||||||
| HGNC | 977 | ||||||
| OMIM | 113530 | ||||||
| RefSeq | NM_001190 | ||||||
| UniProt | O15382 | ||||||
| Other data | |||||||
| EC number | 2.6.1.42 | ||||||
| Locus | Chr. 19 q13 | ||||||
| |||||||
Branched-chain amino acid aminotransferase (BCAT), also known as branched-chain amino acid transaminase, is an aminotransferase enzyme (EC 2.6.1.42) which acts upon branched-chain amino acids (BCAAs). It is encoded by the BCAT2 gene in humans. The BCAT enzyme catalyzes the conversion of BCAAs and α-ketoglutarate into branched chain α-keto acids and glutamate.
The structure to the right of branched chain amino acid aminotransferase was found using X-ray diffraction with a resolution of 2.20 Å. The branched-chain amino acid aminotransferase found in this image was isolated from mycobacteria. This protein is made up of two identical polypeptide chains, totaling 372 residues.
The biological function of branched-chain amino acid aminotransferases is to catalyse the synthesis or degradation of the branched chain amino acids leucine, isoleucine, and valine. In humans, branched chain amino acids are essential and are degraded by BCATs.