A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä

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




TekijätShintani T, Uchiumi T, Yonezawa T, Salminen A, Baykov AA, Lahti R, Hachimori A

KustantajaELSEVIER SCIENCE BV

Julkaisuvuosi1998

JournalFEBS Letters

Tietokannassa oleva lehden nimiFEBS LETTERS

Lehden akronyymiFEBS LETT

Vuosikerta439

Numero3

Aloitussivu263

Lopetussivu266

Sivujen määrä4

ISSN0014-5793

DOIhttps://doi.org/10.1016/S0014-5793(98)01381-7


Tiivistelmä
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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