Properties of Nucleoside Phosphorylase from Enterobacter aerogenes |
| |
| Authors: | Takashi Utagawa Hirokazu Morisawa Shigeru Yamanaka Akihiro Yamazaki Fumihiro Yoshinaga Yoshio Hirose |
| |
| Institution: | Central Research Laboratories, Ajinomoto Co., Inc., 1–1 Suzuki-cho, Kawasaki-ku, Kawasaki 210, Japan |
| |
| Abstract: | The properties of uridine Phosphorylase (UPase) and purine nucleoside Phosphorylase (PNPase) at high temperature were investigated. Both enzymes were found to be distributed in a wide range of bacteria and were partially purified from Enterobacter aerogenes AJ 11125 by heat treatment, ammonium sulfate fractionation and column chromatographies onDEAE-cellulose and Sephadex G-150. The UPase was purified 109-fold, and it showed an optimum pH of 8.5 and optimum temperature of 65°C, and activity toward uridine, 2′-deoxyuridine, thymidine and uracil arabinoside but not cytidine. The Km values of UPase for uridine were 0.7 mm at 40°C and 1.8 mm at 60°C. The PNPase was purified 83-fold, and it showed an optimum pH of 6.8 and optimum temperature of 60°C, and significant activity toward purine arabinosides as well as purine ribosides. The Km values of PNPase for inosine were 0.8 mm at 40°C and 2.2 mm at 60°C. |
| |
| Keywords: | |
|
|
