Purification and Characterization of a Novel (R)-Imine Reductase from Streptomyces sp. GF3587

Koichi MITSUKURA; Mai SUZUKI; Sho SHINODA; Tatsuya KURAMOTO; Toyokazu YOSHIDA; Toru NAGASAWA

doi:10.1271/bbb.110303

Microbiology & Fermentation Technology Regular Papers

Purification and Characterization of a Novel (R)-Imine Reductase from Streptomyces sp. GF3587

Koichi MITSUKURA, Mai SUZUKI, Sho SHINODA, Tatsuya KURAMOTO, Toyokazu YOSHIDA, Toru NAGASAWA

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Keywords: (R)-imine reductase, Streptomyces sp. GF3587, 2-methyl-1-pyrroline, 2-methylpyrrolidine

JOURNAL FREE ACCESS

2011 Volume 75 Issue 9 Pages 1778-1782

DOI https://doi.org/10.1271/bbb.110303

View "Advance Publication" version (September 7, 2011).

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Abstract

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.

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