Purification and characterization of purine nucleoside phosphorylase and pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus TH 6-2.
The purine nucleoside phosphorylase (Pu-NPase) and the pyrimidine nucleoside phosphorylase (Py-NPase) have been purified from Bacillus stearothermophilus TH 6-2. The Pu-NPase is a trimer of 30-kDa subunits and the Py-NPase is a dimer of 46-kDa subunits. The isoelectric points of Pu-NPase and Py-NPase were pH 4.3 and 4.6, respectively. The Pu-NPase could catalyze the phosphorolysis of inosine and guanosine, but not adenosine. the Py-NPase could phosphorolyze both uridine and thymidine.
Hamamoto
T
T
Research & Development Division, Yamasa Corporation, Chiba, Japan.
Noguchi
T
T
Midorikawa
Y
Y
D000595:Amino Acid Sequence; D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D010430:Pentosyltransferases / Q000737:chemistry / Q000302:isolation & purification*; D011683:Purine-Nucleoside Phosphorylase / Q000737:chemistry / Q000302:isolation & purification*; D057845:Pyrimidine Phosphorylases; D013379:Substrate Specificity
D010430:Pentosyltransferases; D057845:Pyrimidine Phosphorylases; D011683:Purine-Nucleoside Phosphorylase