The structure of human mitochondrial branched-chain aminotransferase

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

Research output: Contribution to journalArticlepeer-review

36 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)506-515
Number of pages10
JournalActa Crystallographica Section D: Biological Crystallography
Volume57
Issue number4
DOIs
StatePublished - 2001

All Science Journal Classification (ASJC) codes

  • Structural Biology

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