diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase. Overlapping substrate specificities in a MutT-type protein

• Published in: The Journal of biological chemistry Vol. 274; no. 31; pp. 21735 - 21740
• Main Authors: Safrany, S.T, Ingram, S.W, Cartwright, J.L, Falck, J.R, McLennan, A.G, Barness, L.D, Shears, S.B
• Format: Journal Article
• Language: English
• Published: United States 30.07.1999
• Subjects: Acid Anhydride Hydrolases - chemistry; Acid Anhydride Hydrolases - metabolism; adenosine phosphates; Amino Acid Sequence; Bacillus - enzymology; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Dinucleoside Phosphates - metabolism; enzyme activity; Escherichia coli Proteins; Humans; hydrolysis; Kinetics; Molecular Sequence Data; phosphoric diester hydrolases; Phosphoric Monoester Hydrolases - chemistry; Phosphoric Monoester Hydrolases - metabolism; Pyrophosphatases - chemistry; Pyrophosphatases - metabolism; Saccharomyces cerevisiae; Saccharomyces cerevisiae - enzymology; Schizosaccharomyces - enzymology; Schizosaccharomyces pombe; Schizosaccharomyces pombe Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Substrate Specificity

Aps1 from Schizosaccharomyces pombe (Ingram, S. W., Stratemann, S. A. , and Barnes, L. D. (1999) Biochemistry 38, 3649-3655) and YOR163w from Saccharomyces cerevisiae (Cartwright, J. L., and McLennan, A. G. (1999) J. Biol. Chem. 274, 8604-8610) have both previously been characterized as MutT family...