Cloning and Expression of a Clostridium kluyveri Gene Responsible for Diaphorase Activity
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概要
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A small enzyme showing diaphorase activity was purified from culture supernatant of Clostridium kluyveri and its N-terminal amino acid sequence was determined. This sequence identified a gene (diaA) encoding a protein (DiaA) of 229 amino acids with a predicted molecular weight of 24,981 in the genomic DNA sequence database of C. kluyveri constructed by the Research Institute of Innovative Technology for the Earth. The predicted protein was composed of a flavin reductase-like domain and a rubredoxin-like domain from its N-terminus. The diaA gene was cloned into an expression vector and expressed in an Escherichia coli recombinant. Recombinant enzyme rDiaA showed NADH/NADPH diaphorase activity with 2,6-dichlorophenolindophenol and nitro blue tetrazolium. The enzyme was most active at pH 8.0 at 40 °C. The UV-visible absorption spectrum and thin layer chromatography (TLC) analyses indicated that one rDiaA molecule contained a tightly bound FMN molecule as a prosthetic group. An iron molecule was also detected in an enzyme molecule.
- 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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