A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Evolutionary aspects of inorganic pyrophosphatase
Tekijät: Sivula T, Salminen A, Parfenyev AN, Pohjanjoki P, Goldman A, Cooperman BS, Baykov AA, Lahti R
Kustantaja: ELSEVIER SCIENCE BV
Julkaisuvuosi: 1999
Journal: FEBS Letters
Tietokannassa oleva lehden nimi: FEBS LETTERS
Lehden akronyymi: FEBS LETT
Vuosikerta: 454
Numero: 1-2
Aloitussivu: 75
Lopetussivu: 80
Sivujen määrä: 6
ISSN: 0014-5793
DOI: https://doi.org/10.1016/S0014-5793(99)00779-6
Tiivistelmä
Based on the primary structure, soluble inorganic pyrophosphatases can be divided into two families which exhibit no sequence similarity to each other. Family I, comprising most of the known pyrophosphatase sequences, can be further divided into prokaryotic, plant and animal/fungal pyrophosphatases, Interestingly, plant pyrophosphatases bear a closer similarity to prokaryotic than to animal/fungal pyrophosphatases, Only 17 residues are conserved in all 37 pyrophosphatases of family I and remarkably, 15 of these residues are located at the active site, Subunit interface residues are conserved in animal/fungal but not in prokaryotic pyrophosphatases, (C) 1999 Federation of European Biochemical Societies.
Based on the primary structure, soluble inorganic pyrophosphatases can be divided into two families which exhibit no sequence similarity to each other. Family I, comprising most of the known pyrophosphatase sequences, can be further divided into prokaryotic, plant and animal/fungal pyrophosphatases, Interestingly, plant pyrophosphatases bear a closer similarity to prokaryotic than to animal/fungal pyrophosphatases, Only 17 residues are conserved in all 37 pyrophosphatases of family I and remarkably, 15 of these residues are located at the active site, Subunit interface residues are conserved in animal/fungal but not in prokaryotic pyrophosphatases, (C) 1999 Federation of European Biochemical Societies.
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