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

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

Department of Food Science & Biotechnology

Research output: Contribution to journal › Article › peer-review

20 Scopus citations

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.

Original language	English
Pages (from-to)	14462-14465
Number of pages	4
Journal	Chemical Communications
Volume	55
Issue number	96
DOIs	https://doi.org/10.1039/c9cc06447h
State	Published - 2019

Bibliographical note

Funding Information:
This work was supported by a National Research Foundation of Korea (NRF) grant funded by the Korea government (MEST) (no. 2017008670) and C1 Gas Refinery Research Center (NRF grant number: NRF-2018M3D3A1A01055735) of the National Research Foundation (NRF) of Korea funded by Ministry of Science and ICT.

Publisher Copyright:
This journal is © The Royal Society of Chemistry.

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

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.",

author = "Seo, {Eun Ji} and Kim, {Hye Ji} and Kim, {Myeong Ju} and Kim, {Jeong Sun} and Park, {Jin Byung}",

note = "Funding Information: This work was supported by a National Research Foundation of Korea (NRF) grant funded by the Korea government (MEST) (no. 2017008670) and C1 Gas Refinery Research Center (NRF grant number: NRF-2018M3D3A1A01055735) of the National Research Foundation (NRF) of Korea funded by Ministry of Science and ICT. Publisher Copyright: This journal is {\textcopyright} The Royal Society of Chemistry.",

year = "2019",

doi = "10.1039/c9cc06447h",

language = "English",

volume = "55",

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T2 - Micrococcus luteus for redox-neutral biotransformation of fatty acids

AU - Seo, Eun Ji

AU - Kim, Hye Ji

AU - Kim, Myeong Ju

AU - Kim, Jeong Sun

AU - Park, Jin Byung

N1 - Funding Information: This work was supported by a National Research Foundation of Korea (NRF) grant funded by the Korea government (MEST) (no. 2017008670) and C1 Gas Refinery Research Center (NRF grant number: NRF-2018M3D3A1A01055735) of the National Research Foundation (NRF) of Korea funded by Ministry of Science and ICT. Publisher Copyright: This journal is © The Royal Society of Chemistry.

PY - 2019

Y1 - 2019

N2 - 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.

AB - 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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JO - Chemical Communications

JF - Chemical Communications

IS - 96

ER -

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

Abstract

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