Cloning and expression of a unique inorganic pyrophosphatase from Bacillus subtilis:: evidence for a new family of enzymes

被引：86

作者：

Shintani, T

Uchiumi, T

Yonezawa, T

Salminen, A

Baykov, AA

Lahti, R

Hachimori, A

机构：

[1] Shinshu Univ, Fac Text Sci & Technol, Inst High Polymer Res, Ueda, Nagano 3868856, Japan

[2] Turku Univ, Dept Biochem, FIN-20014 Turku, Finland

[3] Moscow MV Lomonosov State Univ, An Belozersky Inst PhysicoChem Biol, Moscow 119899, Russia

来源：

FEBS LETTERS | 1998年 / 439卷 / 03期

关键词：

pyrophosphatase; exopolyphosphatase; polymerase chain reaction; recombinant enzyme; manganese; Bacillus subtilis;

D O I：

10.1016/S0014-5793(98)01381-7

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：

An open reading frame located in the COTF-TETB intergenic region of Bacillus subtilis was cloned and expressed in Escherichia coli and shown to encode inorganic pyrophosphatase (PPase). The isolated enzyme is Mn2+-activated, like the authentic PPase isolated from B. subtilis. Although 13 functionally important active site residues are conserved in all 31 soluble PPase sequences so far identified, only two of them are conserved in B. subtilis PPase. This suggests that B. subtilis PPase represents a new family of soluble PPases (a Bs family), putative members of which were found in Archaeoglobus fulgidus, Methanococcus jannaschii, Streptococcus mutans and Streptococcus gordonii. (C) 1998 Federation of European Biochemical Societies.

引用

页码：263 / 266

页数：4

共 39 条

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