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Appl. Environ. Microbiol., Nov 1997, 4282-4286, Vol 63, No. 11
Copyright © 1997, American Society for Microbiology

Nucleoside Oxidase, a Hydrogen Peroxide-Forming Oxidase, from Flavobacterium meningosepticum

S Koga, J Ogawa, L Cheng, Y Choi, H Yamada and S Shimizu
Department of Agricultural Chemistry, Kyoto University, Sakyo-ku, Kyoto 606-01, Japan

A novel enzyme which catalyzes the oxidation of nucleosides to nucleoside-5(prm1)-carboxylic acids, forming hydrogen peroxide, was purified to homogeneity from Flavobacterium meningosepticum T-2799. The enzyme has a molecular weight of about 500,000, and four nonidentical subunits (molecular weights of 81,000, 69,000, 33,000, and 16,000) were detected on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. On the basis of visible absorption spectra of the purified enzyme, the enzyme is concluded to be a hemoprotein. It also contains covalently bound flavin adenine dinucleotide. The various nucleosides, such as adenosine (K(infm) = 48 (mu)M), inosine (K(infm) = 66 (mu)M), guanosine (K(infm) = 21 (mu)M), thymidine (K(infm) = 50 (mu)M), uridine (K(infm) = 80 (mu)M), and cytidine (K(infm) = 50 (mu)M), were oxidized by the enzyme, but nucleotides, bases, and ribose were not.

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