Cofactor specificity engineering of a long-chain secondary alcohol dehydrogenase fromMicrococcus luteusfor redox-neutral biotransformation of fatty acids-Reference-Cited by-同舟云学术

Cofactor specificity engineering of a long-chain secondary alcohol dehydrogenase fromMicrococcus luteusfor redox-neutral biotransformation of fatty acids

Published:2019 Issue:96 Volume:55 Page:14462-14465
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Seo Eun-Ji¹²³⁴,Kim Hye-Ji⁵⁶⁷⁴,Kim Myeong-Ju¹²³⁴,Kim Jeong-Sun⁵⁶⁷⁴,Park Jin-Byung¹²³⁴^ORCID

Affiliation:

1. Department of Food Science & Engineering

2. Ewha Womans University

3. Seoul 03760

4. Republic of Korea

5. Department of Chemistry

6. Chonnam National University

7. Gwangju 61186

Abstract

Structure-based cofactor specificity engineering of an alcohol dehydrogenase (mLSADH) enables a redox-neutral biotransformation of C18 fatty acids into C9 fatty acids.

Funder

Ministry of Education, Science and Technology

National Research Foundation of Korea

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2019/CC/C9CC06447H

Reference31 articles.

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2. Biocatalytic Scope of Baeyer–Villiger Monooxygenases

3. Biosynthesis of ω-hydroxy fatty acids and related chemicals from natural fatty acids by recombinant Escherichia coli

4. Co-expression of an alcohol dehydrogenase and a cyclohexanone monooxygenase for cascade reactions facilitates the regeneration of the NADPH cofactor

5. Cascade catalysis – strategies and challenges en route to preparative synthetic biology

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