Nucleoside-Triphosphatase Activity of an ATP-Dependent Enzyme, N-Methylhydantoin Amidohydrolase
スポンサーリンク
概要
- 論文の詳細を見る
N-Methylhydantoin amidohydrolase, which catalyzes ATP-dependent hydrolysis of N-methylhydantoin to N-carbamoylsarcosine, was found to hydrolyze several nucleoside triphosphates to nucleoside diphosphates not only in the presence but also in the absence of amide substrates. Amide substrates, such as N-methylhydantoin and dihydrouracil, seem to be absolutely necessary for hydrolysis of ATP and dATP. However, N-methylhydantoin inhibited the hydrolysis of nucleoside triphosphates other than ATP and dATP. The kinetic data suggest that the presence of an amide substrate changed the affinity of the enzyme toward nucleoside triphosphates.
- 社団法人日本農芸化学会の論文
- 1995-09-23
著者
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Shimizu S
Kyoto Univ. Kyoto Jpn
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SHIMIZU Sakayu
Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University
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YAMADA Hideaki
Department of Agricultural Chemistry, Kyoto University
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Yamada H
Department Of Agricultural Chemistry Facutly Of Agriculture Kyoto University
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Ogawa Jun
Department of Agricultural Chemistry, Kyoto University
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Nirdnoy Warawadee
Department of Agricultural Chemistry, Kyoto University
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Shimizu Sakayu
Department Of Agricultural Chemistry Faculty Of Agriculture Kyoto University
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Yamada H
Department Of Biotechnology Faculty Of Engineering Tottori University
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Yamada H
Res. Inst. Tuberculosis Tokyo Jpn
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Yamada Hideaki
Biotechnology Research Center, Toyama Prefectural University
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Ogawa J
Kyoto Univ. Kyoto Jpn
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Yamada H
Department Of Agricultural Chemistry Kyoto University
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Nirdnoy Warawadee
Department Of Agricultural Chemistry Kyoto University
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Ogawa Jun
Department Of Agricultural Chemistry Kyoto University
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Yamada Hideaki
Department Of Agricultural Chemistry Faculty Of Agriculture Kyoto University
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