Serratia marcescens Purine Nucleoside Phosphorylase의 생합성에 대한 글리옥실산의 대사적 역할

Metabolic Role of Glyoxylate on the Biosynthesis of Serratia marcescens Purine Nucleoside Phosphorylase

The effects of purine catabolites in growth media on the Serratia marcescens purine nucleoside phos-phorylase activity were examined. The enzyme activity was decreased above 60% by guanosine(5 to 15mM). The enzyme activity was not affected at low concentration of inosine (0.1∼1mM). The en-zyme activity was decreased approximately by 40∼50% in the presence of high concentrations of aden-osine hypoxanthine and xanthine (5∼15mM) but was not affected at low concentration of adenosine hypoxanthine and xanthine (0.1∼0.5mM). However the enzyme activity was increase by 20% with low concentrations of uric acid(0.5mN). but was decreased by 80% with high concentrations of same purine catabolite (15mM). Also the enxzyme activity was increased by 20% with low concentrations of glyoxylate (0.5mM) final degradative product of uric acid but was decreased by 30∼50% with high con-centrations of glyoxylate (3∼15mM). The enzyme activity was decreased approximately by 20% by the simultaneous addition of inosine hypoxanthine and uricacid at 5mM each whereas it was increased by 22 and 33% by the combination of inosine and uric acid three purine catabolites at 0.5mM respectively These data suggest that S. marcescens purine nucleoside phosphorylase is positively regulated by a glyox-ylate concentration and then may play a regulatory role in a purine catabolism.