Branched chain aminotransferase
Branched chain aminotransferase is an aminotransferase enzyme which acts upon branched-chain amino acids. It uses largely α-ketoglutarate in forming branched chain α-keto acids and glutamate.
The structure to the right of branched chain aminotransferase was found using X-ray diffraction with a resolution of 2.20 Å. The branched chain aminotransferase found in this image was isolated from mycobacteria. This protein is made up of two identical polypeptide chains. The protein is a total of 372 residues(1). As can be seen in the image, the protein is made of helices and beta sheets.
The biological function of branched chain aminotransferases (BCAT) is to catalyse the synthesis or degradation of the branched chain amino acids leucine, isoleucine, and valine(2). In humans, branched chain amino acids are essential and are degraded by BCATs.
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