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5-Amino-4-imidazole-carboxamide (AICA)-riboside-hydrolyzing enzyme in Bacillus thiaminolyticus AJ 1366 was induced in the presence of uridine, AICA-riboside, xanthosine and inosine. The optimal concentration of AICA-riboside as inducer was 0.4%. This enzyme was produced in parallel with the growth and inactivated in the stationary growth- phase. The substrates were AICA-riboside, adenosine, uridine and inosine. Optimal conditions for hydrolysis of AICA-riboside were pH 7 and at 65°C (40 min). This enzyme was the most stable at pH 8.5 and under 60°C (2 hr). AICA-riboside (1%) was completely hydrolyzed in 4 hr with 50% cultured broth in incubation mixture. Permiability-barrier of AICA-riboside into the cell was observed. The existence of two kinds of AICA-riboside- hydrolyzing enzymes, nucleosidase and Phosphorylase in this bacterium was suggested.

agricultural and biological chemistry

Enzymatic production of 5-amino-4-imidazole-carboxamide from 5-amino-4-imidazole-carboxamide-riboside by Bacillus thiaminolyticus optimal conditions for the enzyme formation and the enzymatic reaction.