Function
Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. Branched chain amino acid catabolism plays a role in adipocyte differentiation by providing lipogenic acetyl-CoA pools in differentiated adipocytes. Mechanistically, acetyl-CoA derived from branched chain amino acid catabolism is used by EP300/p300 to acetylate and inhibit PRDM16, thereby preventing adipose tissue browning.
Biological Context
Subcellular Location: Mitochondrion
Tissue Specificity: Ubiquitous
Disease Association: Hypervalinemia and hyperleucine-isoleucinemia (HVLI) : An autosomal recessive metabolic disorder characterized by highly elevated plasma concentrations of valine and leucine/isoleucine. Affected individuals suffer from headache and mild memory impairment. [The disease is caused by variants affecting the gene represented in this entry. A patient with hypervalinemia and hyperleucine-isoleucinemia was identified as compound heterozygote for Gln-170 (inherited from his father) and Lys-264 (inherited from his mother), both variants reduced the catalytic activity of the enzyme. After treatment with vitamin B6, a precursor of pyridoxal 5'-phosphate, a BCAT2 cofactor, the blood levels of branched chain amino acids, especially valine, were decreased and brain lesions were improved]
Product Specifications
Recombinant Human Branched-chain-amino-acid aminotransferase, mitochondrial (BCAT2) is a recombinant protein from Homo sapiens (Human), expressed in E.coli, covering amino acids 28-392aa, with N-terminal 6xHis-SUMO-tagged tag, molecular weight 57.3kDa, purity Greater than 90% as determined by SDS-PAGE.. Suitable for ELISA and Western Blot applications. Explore more Enzyme proteins →
