Enhancing the atypical esterase promiscuity of the γ-lactamase Sspg from Sulfolobus solfataricusby substrate screening
Wang J, Zhao H, Zhao G, et al
Applied microbiology and biotechnology, 2019, 103(10): 4077-4087
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 characteristics suggest Sspg as a robust enzymatic catalyst for the preparation of optically pure γ-lactam. This study investigated the modification of this enzyme to expand its application toward resolving chiral esters. γ-Lactamase-esterase conversion was performed by employing a three-step method: initial ...
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