首页> 外文期刊>FEBS Letters >Identification of α‐subunit Lys201 and β‐subunit Lys115 at the ATP‐binding sites inEscherichia coli F1‐ATPase
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Identification of α‐subunit Lys201 and β‐subunit Lys115 at the ATP‐binding sites inEscherichia coli F1‐ATPase

机译:在大肠杆菌F1-ATPase的ATP结合位点鉴定α-亚基Lys201和β-亚基Lys115

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>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.
机译:>约1摩尔的三磷酸腺苷三磷酸腺苷与大肠杆菌 F 1 -ATPase的结合导致该酶几乎完全失活[(1987)J. Biol。Chem。化学262,7686–7692]。大约三分之二的标记物与α-亚基结合,其余的与β-亚基结合。本研究表明,α-亚基的Lys 201 和β-亚基的甘氨酸富集区的Lys 155 是该试剂标记的主要位点。因此,这两个残基可能位于结合ATP的γ-磷酸附近。

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