Purification and Characterization of a Novel (R)-Imine Reductase from Streptomyces sp. GF3587
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概要
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The (R)-imine reductase (RIR) of Streptomyces sp. GF3587 was purified and characterized. It was found to be a NADPH-dependent enzyme, and was found to be a homodimer consisting of 32 kDa subunits. Enzymatic reduction of 10 mM 2-methyl-1-pyrroline (2-MPN) resulted in the formation of 9.8 mM (R)-2-methylpyrrolidine ((R)-2-MP) with 99% e.e. The enzyme showed not only reduction activity for 2-MPN at neutral pH (6.5–8.0), but also oxidation activity for (R)-2-MP under alkaline pH (10–11.5) conditions. It appeared to be a sulfhydryl enzyme based on the sensitivity to sulfhydryl specific inhibitors. It was very specific to 2-MPN as substrate.
- 社団法人 日本農芸化学会の論文
著者
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Nagasawa Toru
Department Of Agricultural Chemistry Kyoto University
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Mitsukura Koichi
Department Of Biomolecular Science Gifu University
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Yoshida Toyokazu
Department Of Biomolecular Science Gifu University
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Suzuki Mai
Department Of Applied Physics And Chemistry The University Of Electro-communications
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SHINODA Sho
Department of Biomolecular Science, Faculty of Engineering, Gifu University
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KURAMOTO Tatsuya
Department of Biomolecular Science, Faculty of Engineering, Gifu University
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