Functional Analysis of Aldehyde Oxidase Using Expressed Chimeric Enzyme between Monkey and Rat(Molecular and Cell Biology)
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概要
- 論文の詳細を見る
Aldehyde oxidase (AO) is a homodimer with a subunit molecular mass of approximately 150kDa. Each subunit consists of about 20kDa 2Fe-2S cluster domain storing reducing equivalents, about 40kDa flavine adenine dinucleotide (FAD) domain and about 85kDa molybdenum cofactor (MoCo) domain containing a substrate binding site. In order to clarify the properties of each domain, especially substrate binding domain, chimeric cDNAs were constructed by mutual exchange of 2Fe-2S/FAD and MoCo domains between monkey and rat. Chimeric monkey/rat AO was referred to one with monkey type 2Fe-2S/FAD domains and a rat type MoCo domain. Rat/monkey AO was vice versa. AO-catalyzed 2-oxidation activities of (S)-RS-8359 were measured using the expressed enzyme in Escherichia coli. Substrate inhibition was seen in rat AO and chimeric monkey/rat AO, but not in monkey AO and chimeric rat/monkey AO, suggesting that the phenomenon might be dependent on the natures of MoCo domain of rat. A biphasic Eadie-Hofstee profile was observed in monkey AO and chimeric rat/monkey AO, but not rat AO and chimeric monkey/rat AO, indicating that the biphasic profile might be related to the properties of MoCo domain of monkey. Two-fold greater V_<max> values were observed in monkey AO than in chimeric rat/monkey AO, and in chimeric monkey/rat AO than in rat AO, suggesting that monkey has the more effective electron transfer system than rat. Thus, the use of chimeric enzymes revealed that 2Fe-2S/FAD and MoCo domains affect the velocity and the quantitative profiles of AO-catalyzed (S)-RS-8359 2-oxidation, respectively.
- 公益社団法人日本薬学会の論文
- 2009-01-01
著者
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Tanaka Y
Kyushu Univ. Fukuoka Jpn
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Watanabe Nobuaki
Drug Metabolism And Pharmacokinetics Research Laboratories Daiichi-sankyo Co. Ltd.
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Watanabe Naomi
Department Of Analytical Chemistry Faculty Of Pharmaceutical Sciences Hokuriku University
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Itoh K
Department Of Pharmaceutical Sciences Tohoku University Hospital And Division Of Clinical Pharmacy G
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Itoh Kunio
Department Of Drug Metabolism And Pharmacokinetics Tohoku Pharmaceutical University
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Adachi Mayuko
Department Of Drug Metabolism And Pharmacokinetics Tohoku Pharmaceutical University
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Tanaka Y
Toho Univ. School Of Pharmaceutical Sci. Chiba Jpn
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Tanaka Yorihisa
Department Of Drug Metabolism And Pharmacokinetics Tohoku Pharmaceutical University
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FUKIYA Kensuke
Department of Drug Metabolism and Pharmacokinetics, Tohoku Pharmaceutical University
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ASAKAWA Tasuku
Department of Drug Metabolism and Pharmacokinetics, Tohoku Pharmaceutical University
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HOSHINO Kouichi
Department of Drug Metabolism and Pharmacokinetics, Tohoku Pharmaceutical University
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Fukiya Kensuke
Department Of Drug Metabolism And Pharmacokinetics Tohoku Pharmaceutical University
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Asakawa Tasuku
Department Of Drug Metabolism And Pharmacokinetics Tohoku Pharmaceutical University
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Hoshino Kouichi
Department Of Drug Metabolism And Pharmacokinetics Tohoku Pharmaceutical University
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Tanaka Yorihisa
Department Of Applied Chemistry National Defense Academy
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Tanaka Yoshitaka
Department of Drug Metabolism and Pharmacokinetics, Tohoku Pharmaceutical University
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Itoh Kunio
Department of Biopharmaceutics, Tohoku Pharmaceutical University
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Watanabe Nobuaki
Drug Metabolism and Pharmacokinetics Research Laboratories, Daiichi-Sankyo Co., Ltd.
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