Purifications and Properties of Orotidine-phosphorolyzing Enzyme and Purine Nucleoside Phosphorylase from Erwinia carotovora AJ 2992(Microbiology & Fermentation Industry)
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概要
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An orotidine-phosphorolyzing enzyme and a purine nucleoside phosphorylase (PNPase) of Erwinia carotovora AJ 2992, which is a potent producer of ribavirin (1-β-D-ribofuranosyl-1,2,4-triazole-3-carboxamide), an antiviral agent, from orotidine and 1,2,4-triazole-3-carboxamide (TCA), were purified 23-fold and 103-fold, respectively. At each purification step, the orotidine-phosphorolyzing enzyme was always co-purified with an uridine phosphorylase (UPase) and its activity could not be separated from that of the UPase after it showed as a single band on SDS-polyacrylamide gel electrophoresis. These results suggest that this enzyme may be identical with UPase. The purified enzyme had a molecular weight of 68,000 ±2,000, and seemed to be a dimer. The optimal temperatures and pH values were 60℃ and 6.0 for orotidine phosphorolysis, and 70℃ and 7.0 for uridine phosphorolysis. The Michaelis constants for uridine and orotidine were 0.75mM and 10.87mM, respectively, at 40℃. The PNPase of E. carotovora AJ 2992 had a molecular weight of 58,000±2,000 and seemed to be a dimer. The Michaelis constants for inosine and guanosine were 1.92mM and 1.85mM, respectively, at 40℃. The PNPase was completely inactivated by p-chloromercuribenzoate.
- 社団法人日本農芸化学会の論文
- 1991-07-23
著者
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Yokozeki Kenzo
Central Research Laboratories Of Ajinomoto Co.
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Shirae Hideyuki
Central Research Laboratories Of Ajinomoto Co. Inc.
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