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A carbonyl reductase from Candida parapsilosis ATCC 7330: substrate selectivity and enantiospecificity

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Abstract

Candida parapsilosis ATCC 7330, a rich source of highly stereospecific oxidoreductases, catalyzes oxidation–reduction of a plethora of compounds yielding industrially important intermediates. An (S)-specific carbonyl reductase (SRED) purified and characterized from this yeast is reported here. (R)-Specific carbonyl reductase (CpCR) was reported by us earlier. SRED asymmetrically reduces ketones with excellent enantiospecificity (ee > 99%) and α-ketoesters with higher catalytic activity but moderate enantiospecificity (ee 70%) in the presence of NADPH. Minimal activity is shown towards the reduction of aldehydes. While the reduction of α-ketoesters with SRED can occur with either NADPH or NADH, for ketone reduction SRED requires NADPH specifically. SRED with a subunit molecular weight of 30 kDa shows optimal activity at pH 5.0 and 25 °C, and its activity is affected by Cu2+. Taken together, SRED and CpCR offer substrates which on asymmetric reduction give products of opposite absolute configurations.

Graphical abstract: A carbonyl reductase from Candida parapsilosis ATCC 7330: substrate selectivity and enantiospecificity

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Publication details

The article was received on 13 Feb 2017, accepted on 13 Apr 2017 and first published on 13 Apr 2017


Article type: Paper
DOI: 10.1039/C7OB00340D
Citation: Org. Biomol. Chem., 2017, Advance Article
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    A carbonyl reductase from Candida parapsilosis ATCC 7330: substrate selectivity and enantiospecificity

    S. Sudhakara and A. Chadha, Org. Biomol. Chem., 2017, Advance Article , DOI: 10.1039/C7OB00340D

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