Sivula T, Salminen A, Parfenyev A N, Pohjanjoki P, Goldman A, Cooperman B S, Baykov A A, Lahti R
Department of Biochemistry, University of Turku, Finland.
FEBS Lett. 1999 Jul 2;454(1-2):75-80. doi: 10.1016/s0014-5793(99)00779-6.
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.
