Characteristics of quinolinate phosphoribosyltransferase from the "shiitake" mushroom (Lentinus edodes).
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概要
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A highly purified preparation of quinolinate phosphoribosyltransferase was obtained from the "Shiitake" mushroom and some characteristics of this enzyme were investigated. Maximum activity was observed at an incubation temperature of 50°C. Monovalent cations generally had no effect, but the divalent and trivalent cations were more or less inhibitory. Fe2+, Ni2+, Zn2+, Al3+ and Fe3+ strongly inhibited the reaction and Cl- and NO3- were also inhibitory. The PRPP saturation curve of this enzyme was sigmoidal. PRPP may be an allosteric effector to this enzyme. Quinolinic acid analogues (pyridine di- and mono-carboxylic acids) exerted no influence on the reaction. Some nucleotides were inhibitory, especially ATP, which was the most potent inhibitor. SH reagents and albocycline did not affect the activity. Possible regulations of the de novo biosynthesis of NAD in the mushroom are discussed.
- 財団法人 学会誌刊行センターの論文
著者
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田口 寛
Research Institute for Food Science, Kyoto University
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岩井 和夫
Research Institute for Food Science Kyoto University
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