Engineering substrate promiscuity in 2,4-dichlorophenol hydroxylase by in silico design
Author:
Affiliation:
1. College of Life Science
2. Jilin University
3. Changchun
4. P. R. China
5. Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education
Abstract
In silico designed 2,4-DCP hydroxylase exhibits broader substrate promiscuity for chlorophenols than that of the wild-type enzyme.
Funder
National Natural Science Foundation of China
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemical Engineering,General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2018/RA/C8RA03229G
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1. Biocatalytic Promiscuity
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