Guanosine Deaminase and Guanine Deaminase from Tea Leaves
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概要
- 論文の詳細を見る
Guanosine deaminase and guanine deaminase were partially purified from tea leaves. The optimum activity of guanosine deaminase was observed at pH 7.5 and that of guanine deaminase was at pH 7.0-7.5 and 8.5. Guanosine deaminase was an unstable enzyme. The activities of these deaminases were significantly inhibited by heavy metals. Molecular weights of guanosine deaminase and guanine deaminase as measured by gel filtration were about 18,000 and 54,000, respectively. The K_m for the respective substrates, guanosine and guanine, were 9.5 pM and 41. 7μM. Guanosine deaminase was considered to catalyze the deamination of 2'-deoxyguanosine besides guanosine. It is suggested that guanosine deaminase as well as guanine deaminase in tea leaves not only acts on the catabolic pathway, but also is involved in the biosynthesis of caffeine from guanosine or guanine nucleotides.
- 社団法人日本農芸化学会の論文
- 1994-07-23
著者
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Ozawa T
Univ. Tsukuba Ibaraki Jpn
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Ozawa Tetsuo
Institute Of Applied Biochemistry University Of Tsukuba
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Ozawa T
Tochigi Res. Lab. Kao Corp. Tochigi Jpn
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IMAGAWA Hiroshi
Institute of Applied Biochemistry, University of Tsukuba
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Imagawa Hiroshi
Institute Of Applied Biochemistry University Of Tsukuba
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Imagawa Hiroshi
Faculty Of Pharmaseutical Sciences Tokushima Bunri University
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Imagawa H
Institute Of Applied Biochemistry University Of Tsukuba
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Negishi Osamu
Institute of Applied Biochemistry, University of Tsukuba
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Negishi O
Univ. Tsukuba Ibaraki Jpn
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Negishi Osamu
Institute Of Applied Biochemistry University Of Tsukuba
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Imagawa Hiroshi
Faculty of Pharmaseutical Sciences, Tokushima Bunri University
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