Purification and Characterization of γ-Glutamylcysteine Synthetase of Escherichia coli B(Microbiology & Fermentation Industry)
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概要
- 論文の詳細を見る
γ-Glutamylcysteine synthetase was purified from E. coli B. The enzyme had a molecular weight of 5.5 x 10^4 and required only magnesium ion for activity. The optimal pH and temperature for reaction were 8.5 and 45℃, respectively. The Km values for L-glutamate, L-cysteine, and ATP were 0.50, 0.09, and 0.01 mM, respectively. GTP and UTP were also used as energy sources. The enzyme activity was inhibited by phosphate anions and by various sulfhydryl reagents. Unlike the enzyme from mammalian tissues, the E. coli B enzyme was not inhibited by a-alkyl analogues of methionine. The enzyme was feedback inhibited by reduced glutathione, although oxidized glutathione had no inhibitory effect.
- 社団法人日本農芸化学会の論文
- 1986-08-23
著者
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MURATA KOUSAKU
Research Institute for Food Science, Kyoto University
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KIMURA AKIRA
Research Institute for Food Science, Kyoto University
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Kimura Akira
Research Institute For Food Science Kyoto University
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Kimura A
Hokkaido Univ. Sapporo Jpn
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Watanabe K
Faculty Of Pharmaceutical Science School Of Medicine Fukuoka University
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Murata Kousaku
Research Institute For Food Science Kyoto Univeristy
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WATANABE Kunihiko
Research Institute for Food Science, Kyoto University
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Watanabe Katsunori
Department Of Bioresources Chemistry Faculty Of Horticulture Chiba University
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Watanabe K
Research Institute For Food Science Kyoto University:(present Address)department Of Agricultural Che
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Watanabe K
Marine Biotechnol. Inst. Iwate Jpn
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