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. 2019 Nov 28;55(96):14462-14465.
doi: 10.1039/c9cc06447h.

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

Eun-Ji Seo  1 , Hye-Ji Kim, Myeong-Ju Kim, Jeong-Sun Kim, Jin-Byung Park
Affiliations

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

Eun-Ji Seo et al. Chem Commun (Camb). .

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.

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