Evidence map›Paper›PMID 41184497›Full record

ArticleBiotechnology letters2025

Cloning and characterization of a new oleate hydratase from Acinetobacter ursingii for asymmetric hydration of unactivated alkenes.

Xuan Deng, Yu Wan, Yunyi Li, Xiangyu Wang, Hang Gao, Juan Zhang, Wenchao Gao, Shuangping Huang, Lili Gao, Jiandong Zhang

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Article in Biotechnology letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

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10 authors.

Xuan DengDepartment of Biological and Pharmaceutical Engineering, College of Chemistry and Chemical Engineering, Taiyuan University of Technology, No.79 West Yingze Street, Taiyuan, 030024, Shanxi, China.
Yu WanDepartment of Biological and Pharmaceutical Engineering, College of Chemistry and Chemical Engineering, Taiyuan University of Technology, No.79 West Yingze Street, Taiyuan, 030024, Shanxi, China.
Yunyi LiDepartment of Biological and Pharmaceutical Engineering, College of Chemistry and Chemical Engineering, Taiyuan University of Technology, No.79 West Yingze Street, Taiyuan, 030024, Shanxi, China.
Xiangyu WangDepartment of Biological and Pharmaceutical Engineering, College of Chemistry and Chemical Engineering, Taiyuan University of Technology, No.79 West Yingze Street, Taiyuan, 030024, Shanxi, China.
Hang GaoDepartment of Biological and Pharmaceutical Engineering, College of Chemistry and Chemical Engineering, Taiyuan University of Technology, No.79 West Yingze Street, Taiyuan, 030024, Shanxi, China.
Juan ZhangDepartment of Biological and Pharmaceutical Engineering, College of Chemistry and Chemical Engineering, Taiyuan University of Technology, No.79 West Yingze Street, Taiyuan, 030024, Shanxi, China.
Wenchao GaoDepartment of Biological and Pharmaceutical Engineering, College of Chemistry and Chemical Engineering, Taiyuan University of Technology, No.79 West Yingze Street, Taiyuan, 030024, Shanxi, China.
Shuangping HuangDepartment of Biological and Pharmaceutical Engineering, College of Chemistry and Chemical Engineering, Taiyuan University of Technology, No.79 West Yingze Street, Taiyuan, 030024, Shanxi, China.
Lili GaoCollege of Environment and Ecology, Taiyuan University of Technology, Taiyuan, 030024, Shanxi, China.
Jiandong ZhangDepartment of Biological and Pharmaceutical Engineering, College of Chemistry and Chemical Engineering, Taiyuan University of Technology, No.79 West Yingze Street, Taiyuan, 030024, Shanxi, China. zhangjiandong@tyut.edu.cn.ORCID http://orcid.org/0000-0003-2768-1435

Funding

National Natural Science Foundation of China 22171207
6 · The paper itself

Abstract

objectivesTo expand the availability of promiscuous oleate hydratases (OAHs) for the asymmetric hydration of unactivated alkenes via sequence-based genome mining combined with targeted amino acid substitution.

resultsFrom 100 screened OAHs, 13 candidates were chosen, all exhibiting hydration activity toward oleic acid. These enzymes also showed significant activity with 1-decene (2 mM), with AuOAH, CkOAH, AiOAH, and CeaOAH producing (S)-2-decanol at concentrations of 822, 603, 495, and 461 μM, respectively. AuOAH, CeaOAH, and CkOAH further demonstrated notable activity with short-chain 1-heptene (2 mM), generating (S)-2-heptanol concentrations of 156, 115, and 133 μM, respectively. AuOAH, sourced from Acinetobacter ursingii for its relatively high activity and broad substrate range, was purified and characterized, showing turnover rates of 0.43-3.21 nmol min

conclusionsThis study significantly enriches the enzymatic toolbox for asymmetric alkene hydration and illustrates the beneficial effect of light illumination on OAH-catalyzed hydration.

Indexed as

AcinetobacterAlkenesBacterial ProteinsHydro-LyasesCloning, MolecularEscherichia coliOleic AcidRecombinant ProteinsSubstrate SpecificityAlkenesBacterial ProteinsHydro-LyasesOleic AcidRecombinant ProteinsAlkenesAsymmetric hydrationChiral alcoholsLight-promotedOleate hydratases

Identifiers

PMID41184497

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