Purification and properties of quinolinate phosphoribosyltransferase from the "shitake" mushroom (Lentinus edodes).

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概要

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• A considerably high activity of quinolinate phosphoribosyltransferase, an intermediary enzyme in the de novo NAD biosynthetic pathway, was found in a soluble fraction of the "Shiitake" mushroom extract. Highly purified enzyme (approximately 1, 000-fold, chromatography-cally pure) was extracted for the first time from mushrooms and its general properties were investigated. An apparent molecular weight of 1.6×105 was estimated by the gel filtration method. The optimum pH for the reaction was 6.5. The reaction required a divalent cation in addition to quinolinic acid and PRPP. Michaelis constants for quinolinic acid, PRPP and Mg++ were 1.1×10-5 M, 2.3×10-5M and 2.0×10-4M, respectively. The reaction product was identified as nicotinic acid mononucleotide by KCN addition reaction and by paper partition chromatography.

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著者

• 岩井 和夫

  Research Institute for Food Science, Kyoto University

• 田口 寛

  Research Institute for Food Science, Kyoto University

• 岩井 和夫

  Research Institute for Food Science Kyoto University

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