Glutathione Synthetase of Aspergillus niger : Structural Properties of the Enzyme in Prokaryotes and Eukaryotes(Microbiology & Fermentation Industry)
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概要
- 論文の詳細を見る
Glutathione synthetase isolated from a mold, Aspergillus niger, had a molecular weight of 110,000 and consisted of two apparently identical subunits, each with a molecular weight of 55,000. The enzyme was most active at pH 8.5. It specifically utilized glycine and ATP, and required Mg^<2+> or Mn^<2+> for its catalytic function. A comparison of glutathione synthetases from various sources indicated that the enzyme of eukaryotes (mammals, molds and yeasts) differ from those of prokaryotes (Escherichia coli B and Proteus mirabilis) in molecular structure, although the enzymes from both types of organisms contain an active site thiol and catalyze the same reaction.
- 社団法人日本農芸化学会の論文
- 1989-04-23
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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Murata Kousaku
Research Institute For Food Science Kyoto Univeristy
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Kimura A
Research Institute For Food Science Kyoto University
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YAJIMA NORIO
Asama Kasei Co. Ltd.
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Matsushita Kazunobu
Derartment Of Blological Chemistry Faculty Of Agriculture Yamaguchi University
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