Purification and Properties of Glyoxylate Reductase from Neurospora crassa
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概要
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Three isozymes that catalyze the NADPH-linked reduction of glyoxylate to glycolate were found in cell-free extracts of Neurospora crassa. They were designated glyoxylate reductase-1, 2 and 3 [EC 1.1.1.79]. Glyoxylate reductase-2 was purified about 5400-fold with an activity recovery of 11%, and the purified preparation was electrophoretically homogeneous. The molecular weight was estimated to be 110, 000 by the gel filtration method. The enzyme catalyzed the reduction of glyoxylate and hydroxypyruvate, and was about 4-fold more active with hydroxypyruvate than with glyoxylate at optimum substrate concentration. The enzyme was specific for NADPH as an electron donor, but showed slight affinity towards NADH, and the NADPH: NADH ratio of activity was about 7 : 1. The Michaelis constants for glyoxylate, hydroxypyruvate, NADPH and NADH were found to be 5.7 mM, 85 μM, 3.1 μm and 0.23 mM, respectively. The other isozymes of glyoxylate reductase (GR-1 and 3) differed from GR-2 in molecular size and substrate specificity.
著者
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Tochikura Tatsurokuro
Department Of Agricultural Chemistry Kyoto University
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Moriguchi Mitsuaki
Department Of Applied Chemistry Faculty Of Engineering Oita University
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Kimura Akira
Department Of Anesthesia Obihiro-kosei General Hospital
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MORIGUCHI Mitsuaki
Department of Food Science and Technology, Faculty of Agriculture, Kyoto University
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FUKUDA Hirosuke
Department of Food Science and Technology, Faculty of Agriculture, Kyoto University
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KIMURA Akira
Department of Food Science and Technology, Faculty of Agriculture, Kyoto University
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