Enhancing the atypical esterase promiscuity of the γ-lactamase Sspg from Sulfolobus solfataricus by substrate screening

Promiscuous enzymes can be modified by protein engineering, which enables the catalysis of non-native substrates. γ-lactamase Sspg from Sulfolobus solfataricus is an enzyme with high activity, high stability, and pronounced tolerance of high concentrations of the γ-lactam substrate. These characteri...

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Veröffentlicht in:	Applied microbiology and biotechnology 2019-05, Vol.103 (10), p.4077-4087
Hauptverfasser:	Wang, Jianjun, Zhao, Hongtao, Zhao, Guogang, Chen, Dunfu, Tao, Yong, Wu, Sheng
Format:	Artikel
Sprache:	eng
Schlagworte:	Amides Amidohydrolases - genetics Amidohydrolases - metabolism Catalysis Catalysts Chemical reactions Docking Enantiomers Enzymes Esterase Esters Mass Screening Molecular Docking Simulation Nucleotide sequence Organic chemistry Protein Engineering Proteins Recombinant Proteins - genetics Recombinant Proteins - metabolism Screening Stability Steric hindrance Substrate Specificity Substrates Sulfolobus solfataricus Sulfolobus solfataricus - enzymology
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