Shigella apyrase -: a novel variant of bacterial acid phosphatases?

被引：13

作者：

Babu, MM

Kamalakkannan, S

Subrahmanyam, YVBK

Sankaran, K ^{[1
]}

机构：

[1] Anna Univ, Ctr Biotechnol, Madras 600025, Tamil Nadu, India

[2] Gene Logic Inc, Gaithersburg, MD USA

来源：

FEBS LETTERS | 2002年 / 512卷 / 1-3期

关键词：

pyrophosphatase; acid phosphatase; actin binding; Shigella apyrase; Shigella pathogenesis;

D O I：

10.1016/S0014-5793(02)02287-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A virulence-associated ATP diphosphohydrolase activity in the periplasm of Shigella, identified as apyrase, was found to be markedly similar to bacterial non-specific acid phosphatases in primary structure. When the Shigella apyrase sequence was threaded in to the recently published 3D structure of the highly similar (73%) Escherichia blattae acid phosphatase it was found to have a highly overlapping 3D structure. Our analysis. which included assays for phosphatase, haloperoxidase and catalase activities, led us to hypothesize that Shigella apyrase might belong to a new class of pyrophosphatase originating as one more variant in the family of bacterial non-specific acid phosphatases. It revealed interesting structure-function relationships and probable roles relevant to pathogenesis. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：8 / 12

页数：5

共 23 条

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