Structure-guided protein engineering increases enzymatic activities of the SGNH family esterases

@article{Li2020StructureguidedPE,
  title={Structure-guided protein engineering increases enzymatic activities of the SGNH family esterases},
  author={Zhengyang Li and L. Li and Yingyi Huo and Z. Chen and Yu Zhao and J. Huang and S. Jian and Z. Rong and Dingfeng Wu and J. Gan and Xiaojian Hu and J. Li and X. Xu},
  journal={Biotechnology for Biofuels},
  year={2020},
  volume={13}
}
  • Zhengyang Li, L. Li, +10 authors X. Xu
  • Published 2020
  • Chemistry, Medicine
  • Biotechnology for Biofuels
  • Background Esterases and lipases hydrolyze short-chain esters and long-chain triglycerides, respectively, and therefore play essential roles in the synthesis and decomposition of ester bonds in the pharmaceutical and food industries. Many SGNH family esterases share high similarity in sequences. However, they have distinct enzymatic activities toward the same substrates. Due to a lack of structural information, the detailed catalytic mechanisms of these esterases remain barely investigated… CONTINUE READING

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    References

    SHOWING 1-10 OF 78 REFERENCES
    GDSL family of serine esterases/lipases.
    • 437
    Structural insights of a hormone sensitive lipase homologue Est22
    • 23
    Computational Redesign of Acyl-ACP Thioesterase with Improved Selectivity toward Medium-Chain-Length Fatty Acids.
    • 32
    • PDF
    Probing Enzyme Promiscuity of SGNH Hydrolases
    • 64
    • PDF
    Residue Asn277 Affects the Stability and Substrate Specificity of the SMG1 Lipase from Malassezia globosa
    • 14
    • PDF
    Biochemical characterization of a GDSL-motif esterase from Bacillus sp. K91 with a new putative catalytic mechanism.
    • 8
    • PDF
    Structural and enzymatic characterization of NanS (YjhS), a 9‐O‐Acetyl N‐acetylneuraminic acid esterase from Escherichia coli O157:H7
    • 31