leu, ile, or val + alpha-ketoglutarate <=> a-ketoisocaproate, a-keto-b-methylvalerate, or a-ketoisovalerate + glutamate [BCAT2]

Stable Identifier
Reaction [transition]
Homo sapiens
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Mitochondrial branched-chain-amino-acid aminotransferase (BCAT2) catalyzes the reversible reactions of leucine, isoleucine, or valine with alpha-ketoglutarate (2-oxoglutarate) to form alpha-ketoisocaproate, alpha-keto-beta-methylvalerate, or a-ketoisovalerate, respectively, and glutamate (Bledsoe et al. 1997). The active enzyme is a homodimer (Yennawar et al. 2001, 2002). In the body, this enzyme is widely expressed but is especially abundant in muscle tissue.
Literature References
PubMed ID Title Journal Year
9165094 Cloning of the rat and human mitochondrial branched chain aminotransferases (BCATm)

Hutson, SM, Dawson, PA, Bledsoe, RK

Biochim Biophys Acta 1997
12269802 Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms

Farber, GK, Yennawar, HP, Conway, ME, Hutson, SM, Yennawar, NH

Biochemistry 2002
11264579 The structure of human mitochondrial branched-chain aminotransferase.

Farber, GK, Conway, ME, Hutson, SM, Yennawar, NH, Dunbar, J

Acta Crystallogr D Biol Crystallogr 2001
Catalyst Activity

branched-chain-amino-acid transaminase activity of BCAT2 dimer [mitochondrial matrix]

Orthologous Events
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