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Human mitochondrial branched chain aminotransferase: Structural basis for substrate specificity and role of redox active cysteines (2003)
Journal Article
Yennawar, N., Conway, M. E., Wallin, R., Poole, L. B., & Hutson, S. M. (2003). Human mitochondrial branched chain aminotransferase: Structural basis for substrate specificity and role of redox active cysteines. BBA - Proteins and Proteomics, 1647(1-2), 61-65. https://doi.org/10.1016/S1570-9639%2803%2900051-7

Crystal structures of the fold type IV pyridoxal phosphate (PLP)-dependent human mitochondrial branched chain aminotransferase (hBCATm) reaction intermediates have provided a structural explanation for the kinetically determined substrate specificity... Read More about Human mitochondrial branched chain aminotransferase: Structural basis for substrate specificity and role of redox active cysteines.

Human mitochondrial and cytosolic branched-chain aminotransferases are cysteine S-conjugate β-lyases, but turnover leads to inactivation (2003)
Journal Article
Cooper, A. J. L., Bruschi, S. A., Conway, M., & Hutson, S. M. (2003). Human mitochondrial and cytosolic branched-chain aminotransferases are cysteine S-conjugate β-lyases, but turnover leads to inactivation. Biochemical Pharmacology, 65(2), 181-192. https://doi.org/10.1016/S0006-2952%2802%2901513-7

The mitochondrial and cytosolic branched-chain aminotransferases (BCATm and BCATc) are homodimers in the fold type IV class of pyridoxal 5′-phosphate-containing enzymes that also contains D-amino acid aminotransferase and 4-amino-4-deoxychorismate ly... Read More about Human mitochondrial and cytosolic branched-chain aminotransferases are cysteine S-conjugate β-lyases, but turnover leads to inactivation.