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Cofactor specificity engineering of a long-chain secondary alcohol dehydrogenase from Micrococcus luteus for redox-neutral biotransformation of fatty acids

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Abstract

Structure-based engineering of a NAD+-dependent secondary alcohol dehydrogenase from Micrococcus luteus led to a 1800-fold increase in catalytic efficiency for NADP+. Furthermore, the engineered enzymes (e.g., D37S/A38R/V39S/T15I) were successfully coupled to a NADPH-dependent Baeyer–Villiger monooxygenase from Pseudomonas putida KT2440 for redox-neutral biotransformations of C18 fatty acids into C9 chemicals.

Graphical abstract: Cofactor specificity engineering of a long-chain secondary alcohol dehydrogenase from Micrococcus luteus for redox-neutral biotransformation of fatty acids

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Publication details

The article was received on 20 Aug 2019, accepted on 01 Nov 2019 and first published on 01 Nov 2019


Article type: Communication
DOI: 10.1039/C9CC06447H
Chem. Commun., 2019, Advance Article

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    Cofactor specificity engineering of a long-chain secondary alcohol dehydrogenase from Micrococcus luteus for redox-neutral biotransformation of fatty acids

    E. Seo, H. Kim, M. Kim, J. Kim and J. Park, Chem. Commun., 2019, Advance Article , DOI: 10.1039/C9CC06447H

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