Tagaya M, Noumi T, Nakano K, Futai M, Fukui T
Institute of Scientific and Industrial Research, Osaka University, Japan.
FEBS Lett. 1988 Jun 20;233(2):347-51. doi: 10.1016/0014-5793(88)80457-5.
Binding of about 1 mol of adenosine triphosphopyridoxal to Escherichia coli F1-ATPase resulted in the nearly complete inactivation of the enzyme [(1987) J. Biol. Chem. 262, 7686-7692]. About two thirds of the label was bound to the alpha-subunit, and the rest to the beta-subunit. The present study revealed that Lys201 in the alpha-subunit and Lys155 in the glycine-rich region of the beta-subunit are the major sites labeled with this reagent. Thus, these two residues might be located close to the gamma-phosphate of the bound ATP.
约1摩尔三磷酸吡啶醛腺苷与大肠杆菌F1 - ATP酶结合导致该酶几乎完全失活[（1987年）《生物化学杂志》262卷，7686 - 7692页]。约三分之二的标记物结合到α亚基上，其余的结合到β亚基上。本研究表明，α亚基中的赖氨酸201和β亚基富含甘氨酸区域中的赖氨酸155是被该试剂标记的主要位点。因此，这两个残基可能位于结合的ATP的γ - 磷酸基团附近。
