A1 Refereed original research article in a scientific journal
Cloning and expression of a unique inorganic pyrophosphatase from Bacillus subtilis: evidence for a new family of enzymes
Authors: Shintani T, Uchiumi T, Yonezawa T, Salminen A, Baykov AA, Lahti R, Hachimori A
Publisher: ELSEVIER SCIENCE BV
Publication year: 1998
Journal: FEBS Letters
Journal name in source: FEBS LETTERS
Journal acronym: FEBS LETT
Volume: 439
Issue: 3
First page : 263
Last page: 266
Number of pages: 4
ISSN: 0014-5793
DOI: https://doi.org/10.1016/S0014-5793(98)01381-7
Abstract
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.
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.
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