钴对大肠杆菌5'-核苷酸酶的激活作用是由于仅在两个金属离子结合位点中的一个位点上锌离子被取代。
Cobalt activation of Escherichia coli 5'-nucleotidase is due to zinc ion displacement at only one of two metal-ion-binding sites.
作者信息
McMillen Lyle, Beacham Ifor R, Burns Dennis M
机构信息
School of Biomolecular and Biomedical Science, Faculty of Science, Griffith University, Nathan, Brisbane, Queensland 4111, Australia.
出版信息
Biochem J. 2003 Jun 1;372(Pt 2):625-30. doi: 10.1042/BJ20021800.
Abstract
Escherichia coli 5'-nucleotidase activity is stimulated 30- to 50-fold in vitro by the addition of Co(2+). Seven residues from conserved sequence motifs implicated in the catalytic and metal-ion-binding sites of E. coli 5'-nucleotidase (Asp(41), His(43), Asp(84), His(117), Glu(118), His(217) and His(252)) were selected for modification using site-directed mutagenesis of the cloned ushA gene. On the basis of comparative studies between the resultant mutant proteins and the wild-type enzyme, a model is proposed for E. coli 5'-nucleotidase in which a Co(2+) ion may displace the Zn(2+) ion at only one of two metal-ion-binding sites; the other metal-ion-binding site retains the Zn(2+) ion already present. The studies reported herein suggest that displacement occurs at the metal-ion-binding site consisting of residues Asp(84), Asn(116), His(217) and His(252), leading to the observed increase in 5'-nucleotidase activity.
摘要
通过添加Co(2+)，大肠杆菌5'-核苷酸酶活性在体外被刺激30至50倍。从与大肠杆菌5'-核苷酸酶催化和金属离子结合位点相关的保守序列基序中选择了七个残基（Asp(41)、His(43)、Asp(84)、His(117)、Glu(118)、His(217)和His(252)），使用克隆的ushA基因的定点诱变进行修饰。基于所得突变蛋白与野生型酶之间的比较研究，提出了一种大肠杆菌5'-核苷酸酶的模型，其中Co(2+)离子可能仅在两个金属离子结合位点之一取代Zn(2+)离子；另一个金属离子结合位点保留已存在的Zn(2+)离子。本文报道的研究表明，取代发生在由Asp(84)、Asn(116)、His(217)和His(252)残基组成的金属离子结合位点，导致观察到的5'-核苷酸酶活性增加。
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