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Shigella apyrase – a novel variant of bacterial acid phosphatases?
Author(s) -
Babu M.Madan,
Kamalakkannan S,
Subrahmanyam Yerramalli V.B.K,
Sankaran Krishnan
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02287-1
Subject(s) - apyrase , phosphatase , biochemistry , shigella , acid phosphatase , biology , periplasmic space , escherichia coli , microbiology and biotechnology , peptide sequence , chemistry , enzyme , gene
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.