Artificial cysteine-lipases with high activity and altered catalytic mechanism created by laboratory evolution

Candida antarctica lipase B (CALB) is a serine lipase. Here, the authors use directed evolution to exchange serine with cysteine in the catalytic triad of the enzyme, thereby obtaining a highly active CALB variant that — unlike the wild type — accommodates bulky substrates.

Bibliographic Details
Published in:Nature Communications
Main Authors: Yixin Cen, Warispreet Singh, Mamatjan Arkin, Thomas S. Moody, Meilan Huang, Jiahai Zhou, Qi Wu, Manfred T. Reetz
Format: Article in Journal/Newspaper
Language:English
Published: Nature Portfolio 2019
Subjects:
Science
Q
Antarc*
Antarctica
Online Access:https://doi.org/10.1038/s41467-019-11155-3
https://doaj.org/article/382d844422024dc1aad5ab0dfe4e992c
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spelling ftdoajarticles:oai:doaj.org/article:382d844422024dc1aad5ab0dfe4e992c 2023-05-15T13:48:04+02:00 Artificial cysteine-lipases with high activity and altered catalytic mechanism created by laboratory evolution Yixin Cen Warispreet Singh Mamatjan Arkin Thomas S. Moody Meilan Huang Jiahai Zhou Qi Wu Manfred T. Reetz 2019-07-01T00:00:00Z https://doi.org/10.1038/s41467-019-11155-3 https://doaj.org/article/382d844422024dc1aad5ab0dfe4e992c EN eng Nature Portfolio https://doi.org/10.1038/s41467-019-11155-3 https://doaj.org/toc/2041-1723 doi:10.1038/s41467-019-11155-3 2041-1723 https://doaj.org/article/382d844422024dc1aad5ab0dfe4e992c Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019) Science Q article 2019 ftdoajarticles https://doi.org/10.1038/s41467-019-11155-3 2022-12-31T04:18:29Z Candida antarctica lipase B (CALB) is a serine lipase. Here, the authors use directed evolution to exchange serine with cysteine in the catalytic triad of the enzyme, thereby obtaining a highly active CALB variant that — unlike the wild type — accommodates bulky substrates. Article in Journal/Newspaper Antarc* Antarctica Directory of Open Access Journals: DOAJ Articles Nature Communications 10 1
institution Open Polar
collection Directory of Open Access Journals: DOAJ Articles
op_collection_id ftdoajarticles
language English
topic Science
Q
spellingShingle Science
Q
Yixin Cen
Warispreet Singh
Mamatjan Arkin
Thomas S. Moody
Meilan Huang
Jiahai Zhou
Qi Wu
Manfred T. Reetz
Artificial cysteine-lipases with high activity and altered catalytic mechanism created by laboratory evolution
topic_facet Science
Q
description Candida antarctica lipase B (CALB) is a serine lipase. Here, the authors use directed evolution to exchange serine with cysteine in the catalytic triad of the enzyme, thereby obtaining a highly active CALB variant that — unlike the wild type — accommodates bulky substrates.
format Article in Journal/Newspaper
author Yixin Cen
Warispreet Singh
Mamatjan Arkin
Thomas S. Moody
Meilan Huang
Jiahai Zhou
Qi Wu
Manfred T. Reetz
author_facet Yixin Cen
Warispreet Singh
Mamatjan Arkin
Thomas S. Moody
Meilan Huang
Jiahai Zhou
Qi Wu
Manfred T. Reetz
author_sort Yixin Cen
title Artificial cysteine-lipases with high activity and altered catalytic mechanism created by laboratory evolution
title_short Artificial cysteine-lipases with high activity and altered catalytic mechanism created by laboratory evolution
title_full Artificial cysteine-lipases with high activity and altered catalytic mechanism created by laboratory evolution
title_fullStr Artificial cysteine-lipases with high activity and altered catalytic mechanism created by laboratory evolution
title_full_unstemmed Artificial cysteine-lipases with high activity and altered catalytic mechanism created by laboratory evolution
title_sort artificial cysteine-lipases with high activity and altered catalytic mechanism created by laboratory evolution
publisher Nature Portfolio
publishDate 2019
url https://doi.org/10.1038/s41467-019-11155-3
https://doaj.org/article/382d844422024dc1aad5ab0dfe4e992c
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_source Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
op_relation https://doi.org/10.1038/s41467-019-11155-3
https://doaj.org/toc/2041-1723
doi:10.1038/s41467-019-11155-3
2041-1723
https://doaj.org/article/382d844422024dc1aad5ab0dfe4e992c
op_doi https://doi.org/10.1038/s41467-019-11155-3
container_title Nature Communications
container_volume 10
container_issue 1
_version_ 1766248559836921856

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