Purification and characterization of purine nucleoside phosphorylase and pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus TH 6-2

Biosci Biotechnol Biochem. 1996 Jul;60(7):1179-80. doi: 10.1271/bbb.60.1179.


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.

MeSH terms

  • Amino Acid Sequence
  • Chromatography, DEAE-Cellulose
  • Electrophoresis, Polyacrylamide Gel
  • Geobacillus stearothermophilus / enzymology*
  • Hydrogen-Ion Concentration
  • Isoelectric Focusing
  • Molecular Sequence Data
  • Pentosyltransferases / chemistry
  • Pentosyltransferases / isolation & purification*
  • Purine-Nucleoside Phosphorylase / chemistry
  • Purine-Nucleoside Phosphorylase / isolation & purification*
  • Pyrimidine Phosphorylases
  • Substrate Specificity


  • Pentosyltransferases
  • Pyrimidine Phosphorylases
  • Purine-Nucleoside Phosphorylase