期刊论文详细信息
FEBS Letters
Identification of α‐subunit Lys201 and β‐subunit Lys115 at the ATP‐binding sites inEscherichia coli F1‐ATPase
Futai, Masamitsu1  Tagaya, Mitsuo1  Noumi, Takato1  Nakano, Kenichi1  Fukui, Toshio1 
[1] Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567, Japan
关键词: F1-ATPase;    Nucleotide-binding site;    Affinity label;    Adenosine polyphosphopyridoxal;    Glycine-rich region;    AP3-PL;    adenosine triphosphopyridoxal;    FSBA;    5′-p-fluorosulfonylbenzoyl adenosine;    FSBI;    5′-p-fluorosulfonylbenzoyl inosine;    HPLC;    high performance liquid chromatography;   
DOI  :  10.1016/0014-5793(88)80457-5
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

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 α-subunit, and the rest to the β-subunit. The present study revealed that Lys201 in the α-subunit and Lys155 in the glycinerich region of the β-subunit are the major sites labeled with this reagent. Thus, these two residues might be located close to the γ-phosphate of the bound ATP.

【 授权许可】

Unknown   

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