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A novel SGNH family hydrolase Ali5 with thioesterase activity and a GNSL motif but without a classic GDSL motif from Altererythrobacter ishigakiensis

Authors
  • Hong, Li-Guo1, 2, 3
  • Jian, Shu-Ling2, 3
  • Huo, Ying-Yi2, 3, 4
  • Cheng, Hong2, 3
  • Hu, Xiao-Jian5
  • Li, Jixi5
  • Cui, Heng-Lin1
  • Xu, Xue-Wei2, 3
  • 1 Jiangsu University, School of Food and Biological Engineering, 301 Xuefu Road, Jingkou District, Zhenjiang, 212013, People’s Republic of China , Zhenjiang (China)
  • 2 State Oceanic Administration, Key Laboratory of Marine Ecosystem and Biogeochemistry, Hangzhou, 310012, People’s Republic of China , Hangzhou (China)
  • 3 Ministry of Natural Resources, Second Institute of Oceanography, 36 North Baochu Road, Hangzhou, 310012, People’s Republic of China , Hangzhou (China)
  • 4 Zhejiang University, Teaching Center of Biological Experiments, Hangzhou, 310058, People’s Republic of China , Hangzhou (China)
  • 5 Shanghai Engineering Research Center of Industrial Microorganisms, Fudan University, State Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, School of Life Sciences, Shanghai, 200438, People’s Republic of China , Shanghai (China)
Type
Published Article
Journal
Biotechnology Letters
Publisher
Springer-Verlag
Publication Date
Mar 20, 2019
Volume
41
Issue
4-5
Pages
591–604
Identifiers
DOI: 10.1007/s10529-019-02662-w
Source
Springer Nature
Keywords
License
Yellow

Abstract

ObjectiveWe aimed to characterize a novel SGNH (Ser-Gly-Asn-His) family hydrolase from the annotated genome of marine bacteria with new features.ResultsA novel esterase Ali5 from Altererythrobacter ishigakiensis has been identified and classified into SGNH family. Ali5 presented a novel GNSL (Gly-Asn-Ser-Leu(X)) motif that differs from the classic GDSL (Gly-Asp-Ser-Leu(X)) motif of SGNH family. The enzyme has esterase and thioesterase activity and exhibited apparent temperature and pH optima of 40 °C and pH 7.5 (in phosphate buffer), respectively. Ali5 was found to be halotolerant and thermostable, and exhibited strong resistance to several organic solvents and metal ions. The residue Tyr196 has a great influence on the catalytic activity, which was proved by site-directed mutagenesis and subsequent kinetic characterization.ConclusionThe esterase Ali5 with esterase and thioesterase activities, salt and metal ions resistance and unique structural features was identified, which holds promise for research on the SGNH family of hydrolases.

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