Characterization of a Dihydrolipoyl Dehydrogenase Having Diaphorase Activity of Clostridium kluyveri
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概要
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The Clostridium kluyveri bfmBC gene encoding a putative dihydrolipoyl dehydrogenase (DLD; EC 1.8.1.4) was expressed in Escherichia coli, and the recombinant enzyme rBfmBC was characterized. UV-visible absorption spectrum and thin layer chromatography analysis of rBfmBC indicated that the enzyme contained a noncovalently but tightly attached FAD molecule. rBfmBC catalyzed the oxidation of dihydrolipoamide (DLA) with NAD+ as a specific electron acceptor, and the apparent Km values for DLA and NAD+ were 0.3 and 0.5 mM respectively. In the reverse reaction, the apparent Km values for lipoamide and NADH were 0.42 and 0.038 mM respectively. Like other DLDs, this enzyme showed NADH dehydrogenase (diaphorase) activity with some synthetic dyes, such as 2,6-dichlorophenolindophenol and nitro blue tetrazolium. rBfmBC was optimally active at 40 °C at pH 7.0, and the enzyme maintained some activity after a 30-min incubation at 60 °C.
- 社団法人 日本農芸化学会の論文
著者
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Kajino T
Special Research Laboratory Ii Toyota Central R&d Laboratories Inc.
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Sakka Kazuo
Graduate School Of Bioresources Mie Univ.
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Kimura Tetsuya
Graduate School Of Human & Environmental Studies Kyoto University
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Sakka Makiko
Graduate School Of Bioresources Mie Univ.
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CHAKRABORTY Saikat
Graduate School of Bioresources, Mie University
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