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

Eun-Ji Seo; Hye-Ji Kim; Myeong-Ju Kim; Jeong-Sun Kim; Jin-Byung Park

doi:10.1039/c9cc06447h

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

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

Authors

Eun-Ji Seo¹, Hye-Ji Kim, Myeong-Ju Kim, Jeong-Sun Kim, Jin-Byung Park

Affiliation

¹ Department of Food Science & Engineering, Ewha Womans University, Seoul 03760, Republic of Korea. [email protected].

PMID: 31728457
DOI: 10.1039/c9cc06447h

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.

MeSH terms

Alcohol Oxidoreductases / chemistry
Alcohol Oxidoreductases / genetics
Alcohol Oxidoreductases / metabolism*
Binding Sites
Biotransformation
Fatty Acids / metabolism
Genetic Engineering
Kinetics
Micrococcus luteus / enzymology*
Mixed Function Oxygenases / metabolism
Molecular Dynamics Simulation
Oxidation-Reduction
Pseudomonas / enzymology

Substances

Fatty Acids
Mixed Function Oxygenases
Alcohol Oxidoreductases
isopropanol dehydrogenase (NADP)