Cloning and expression of a unique inorganic pyrophosphatase from Bacillus subtilis: evidence for a new family of enzymes.
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.
Shintani
T
T
Institute of High Polymer Research, Faculty of Textile Science and Technology, Shinshu University, Ueda, Nagano, Japan.
Uchiumi
T
T
Yonezawa
T
T
Salminen
A
A
Baykov
A A
AA
Lahti
R
R
Hachimori
A
A
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology / Q000235:genetics*; D003001:Cloning, Molecular; D004926:Escherichia coli; D015870:Gene Expression; D043564:Inorganic Pyrophosphatase; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D016133:Polymerase Chain Reaction; D011755:Pyrophosphatases / Q000235:genetics* / Q000302:isolation & purification; D017386:Sequence Homology, Amino Acid
D011755:Pyrophosphatases; D043564:Inorganic Pyrophosphatase