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Cloning and expression of a unique inorganic pyrophosphatase from Bacillus subtilis : evidence for a new family of enzymes
Author(s) -
Shintani Toshio,
Uchiumi Toshio,
Yonezawa Tomoki,
Salminen Anu,
Baykov Alexander A.,
Lahti Reijo,
Hachimori Akira
Publication year - 1998
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(98)01381-7
Subject(s) - bacillus subtilis , methanococcus , inorganic pyrophosphatase , escherichia coli , biochemistry , open reading frame , streptococcus gordonii , biology , enzyme , pyrophosphatases , pyrophosphatase , cloning (programming) , genetics , gene , bacteria , peptide sequence , streptococcus , pyrophosphate , computer science , programming language
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 Mn 2+ ‐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 .