InChI=1S/C5H11N/c1-5-3-2-4-6-5/h5-6H,2-4H2,1H3/p+1/t5-/m1/s1 |
RGHPCLZJAFCTIK-RXMQYKEDSA-O |
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(2R)-2-methylpyrrolidinium
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(R)-2-methylpyrrolidine
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UniProt
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(R)-2-methylpyrrolidine(1+)
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ChEBI
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(R)-2-MP
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SUBMITTER
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Mitsukura K, Suzuki M, Shinoda S, Kuramoto T, Yoshida T, Nagasawa T (2011) Purification and characterization of a novel (R)-imine reductase from Streptomyces sp. GF3587. Bioscience, biotechnology, and biochemistry 75, 1778-1782 (Source: SUBMITTER) [PubMed:21897027] [show 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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