The structure of human mitochondrial branched-chain aminotransferase

Hutson, S.; Farber, G.; Yennawar, N.; Conway, M.; Hutson, Susan M.; Dunbar, J.; Farber, J

Abstract

X-ray crystal structures of three forms of human mitochondrial branched-chain aminotransferase were solved by molecular-replacement methods. In two of the forms the enzyme is in its active form, with the pyridoxal 5′-phosphate (PLP) cofactor covalently linked to the ε-amino group of the active-site lysine. In the third form, a molecule of the Tris buffer is covalently bound to the PLP on one end and the active-site lysine on the other, inhibiting the enzyme irreversibly.

• Journal Article Type: Article
• Publication Date: Apr 25, 2001
• Journal: Acta Crystallographica Section D: Biological Crystallography
• Print ISSN: 0907-4449
• Publisher: International Union of Crystallography
• Peer Reviewed: Peer Reviewed
• Volume: 57
• Issue: 4
• Pages: 506-515
• DOI: https://doi.org/10.1107/S0907444901001925
• Keywords: aminotransferases, inhibitors
• Public URL: https://uwe-repository.worktribe.com/output/1087181
• Publisher URL: http://dx.doi.org/10.1107/S0907444901001925