Evidence map›Paper›PMID 40531301›Full record

ArticleApplied biochemistry and biotechnology2025

A Novel Esterase from Burkholderia sp. YD106 Capable of Hydrolysis of Methyl (R, S)-N-(2, 6-Dimethylphenyl) Alaninate, and Its Mutation for Improving Enantioselectivity.

Ruixue Yang, Jianing Wu, Yunhe Zhang, Zhaohui Zhang

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Article in Applied biochemistry and biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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1citing papers in PubMed
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1 · What the graph read from it

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3 · Its place in the literature

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1 citing paper in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

4 authors.

Ruixue YangCollege of Biological Engineering, Zhejiang University of Technology, Zhejiang Province 310014, Hangzhou, People's Republic of China.
Jianing WuCollege of Biological Engineering, Zhejiang University of Technology, Zhejiang Province 310014, Hangzhou, People's Republic of China.
Yunhe ZhangZhejiang University-University of Edinburgh Institute (ZJU-UoE Institute), Zhejiang University, Zhejiang Province, Haining, 314400, China.
Zhaohui ZhangCollege of Biological Engineering, Zhejiang University of Technology, Zhejiang Province 310014, Hangzhou, People's Republic of China. zzh@zjut.edu.cn.ORCID http://orcid.org/0009-0002-4766-1140

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Methyl (R, S)-2, 6-dimethylphenylaminopropionate ((R, S)-1) is an intermediate in the production of the agricultural fungicide (R, S)-metalaxyl. (R, S)-1 can be hydrolyzed enantioselectively by some hydrolases to produce (R)-1, which was used for the production of (R)-metalaxyl. In this work, a strain Burkholderia sp. YD106 that could hydrolyze (R, S)-1 was screened from the activated sludge, but it had almost no enantioselectivity. The intracellular active esterase WZest was successfully heterologously expressed in the recombinant E. coli BL21 (DE3)-pET-28a ( +)-GE04845. Using the recombinant strain as the parent strain, the mutants were constructed by a site-directed mutation. Among all 33 mutants, seven had altered enantioselectivity, of which four mutants were (R)-enantioselective and three were (S)-enantioselective. The mutant WZest-W23T had the highest (R)-enantioselectivity. When it catalyzed the hydrolysis of (R, S)-1 at 44.6% substrate conversion, e.e.

Indexed as

AlanineBurkholderiaEsterasesMutationEscherichia coliHydrolysisMutagenesis, Site-DirectedStereoisomerismSubstrate SpecificityAlanineEsterases6-dimethylphenylaminopropionateEnantioselectivityEsteraseMethyl (R, S)-2(R)-metalaxylSite-directed mutantStrain screening

Identifiers

PMID40531301

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