大肠杆菌多聚磷酸激酶中的磷酸组氨酰活性位点。
Phosphohistidyl active sites in polyphosphate kinase of Escherichia coli.
作者信息
Kumble K D, Ahn K, Kornberg A
机构信息
Department of Biochemistry, Beckman Center, Stanford University School of Medicine, CA 94305-5307, USA.
出版信息
Proc Natl Acad Sci U S A. 1996 Dec 10;93(25):14391-5. doi: 10.1073/pnas.93.25.14391.
Abstract
In the synthesis of inorganic polyphosphate (polyP) from ATP by polyphosphate kinase (PPK; EC 2.7.4.1) of Escherichia coli, an N-P-linked phosphoenzyme was previously identified as the intermediate. The phosphate is presumed to be linked to N3 of the histidine residue because of its chemical stabilities and its resemblance to other enzymes known to contain N3-phosphohistidine. Tryptic digests of [32P]PPK contain a predominant 32P-labeled peptide that includes His-441. Of the 16 histidine residues in PPK of E. coli, 4 are conserved among several bacterial species. Mutagenesis of these 4 histidines shows that two (His-430 and His-598) are unaffected in function when mutated to glutamine, whereas two others (His-441 and His-460) mutated to glutamine or alanine fail to be phosphorylated, show no enzymatic activities, and fail to support polyP accumulation in cells bearing these mutant enzymes.
摘要
在大肠杆菌的多聚磷酸激酶（PPK；EC 2.7.4.1）由ATP合成无机多聚磷酸（polyP）的过程中，一种N-P连接的磷酸化酶先前被鉴定为中间体。由于其化学稳定性以及与已知含有N3-磷酸组氨酸的其他酶的相似性，推测该磷酸盐与组氨酸残基的N3相连。[32P]PPK的胰蛋白酶消化产物包含一种主要的32P标记肽，其中包括His-441。在大肠杆菌PPK的16个组氨酸残基中，有4个在几种细菌物种中是保守的。对这4个组氨酸进行诱变表明，其中两个（His-430和His-598）突变为谷氨酰胺时功能不受影响，而另外两个（His-441和His-460）突变为谷氨酰胺或丙氨酸时则无法被磷酸化，没有酶活性，并且在携带这些突变酶的细胞中无法支持多聚磷酸的积累。
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