A1 Refereed original research article in a scientific journal
Evolutionary aspects of inorganic pyrophosphatase
Authors: Sivula T, Salminen A, Parfenyev AN, Pohjanjoki P, Goldman A, Cooperman BS, Baykov AA, Lahti R
Publisher: ELSEVIER SCIENCE BV
Publication year: 1999
Journal: FEBS Letters
Journal name in source: FEBS LETTERS
Journal acronym: FEBS LETT
Volume: 454
Issue: 1-2
First page : 75
Last page: 80
Number of pages: 6
ISSN: 0014-5793
DOI: https://doi.org/10.1016/S0014-5793(99)00779-6
Abstract
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.
UTU Research Portal