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细菌蛋白激酶/磷酸酶NRII自身磷酸化位点的鉴定。

Identification of the site of autophosphorylation of the bacterial protein kinase/phosphatase NRII.

作者信息

Ninfa A J, Bennett R L

机构信息

Department of Biochemistry, Wayne State University School of Medicine, Detroit, Michigan 48201.

出版信息

J Biol Chem. 1991 Apr 15;266(11):6888-93.

PMID:2016302
Abstract

Previous studies have established that the Escherichia coli protein kinase/phosphatase nitrogen regulator II (NRII also known as NtrB) becomes autophosphorylated on a histidine residue when incubated with ATP. We show that the major site at which NRII was autophosphorylated was contained within a peptide consisting of amino acid residues 136-142 of NRII, and thus probably corresponds to His-139. A minor site of phosphorylation, accounting for about 2% of the phosphate in NRII-P, was found in a peptide that corresponds to residues 158-169.

摘要

以往的研究已证实，大肠杆菌蛋白激酶/磷酸酶氮调节因子II（NRII，也称为NtrB）与ATP一起温育时，会在一个组氨酸残基上发生自磷酸化。我们发现，NRII自磷酸化的主要位点位于由NRII的氨基酸残基136 - 142组成的肽段内，因此可能对应于His-139。在一个对应于残基158 - 169的肽段中发现了一个次要的磷酸化位点，约占NRII-P中磷酸盐的2%。

相似文献

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Identification of the site of autophosphorylation of the bacterial protein kinase/phosphatase NRII.细菌蛋白激酶/磷酸酶NRII自身磷酸化位点的鉴定。
J Biol Chem. 1991 Apr 15;266(11):6888-93.
2
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Crystal structure of the C-terminal domain of the two-component system transmitter protein nitrogen regulator II (NRII; NtrB), regulator of nitrogen assimilation in Escherichia coli.大肠杆菌氮同化调节因子、双组分系统信号转导蛋白氮调节因子II（NRII；NtrB）C端结构域的晶体结构
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