TY - JOUR
T1 - The structure of human mitochondrial branched-chain aminotransferase
AU - Yennawar, N.
AU - Dunbar, J.
AU - Conway, M.
AU - Hutson, S.
AU - Farber, G.
PY - 2001
Y1 - 2001
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0035075262&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035075262&partnerID=8YFLogxK
U2 - 10.1107/S0907444901001925
DO - 10.1107/S0907444901001925
M3 - Article
C2 - 11264579
AN - SCOPUS:0035075262
VL - 57
SP - 506
EP - 515
JO - Acta Crystallographica Section D: Structural Biology
JF - Acta Crystallographica Section D: Structural Biology
SN - 0907-4449
IS - 4
ER -