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- W3048754954 abstract "Abstract Engineering active sites in inert scaffolds to catalyze chemical transformations with unnatural substrates is still a great challenge for enzyme catalysis. In this research, a p-nitrobenzyl esterase from Bacillus subtilis was identified from the structural database, and a double mutant E115A/E188A was designed to afford catalytic activities toward the hydrolysis of ceftizoxime. A quadruple mutant E115A/E188A/L362S/I270A with enhanced catalytic efficiency was created to catalyze the condensation reaction of ethyl-2-methoxy-amino-2-(2-aminothiazole-4-yl) acetate with 7-amino-3-nor-cephalosporanic acid to produce ceftizoxime in a fully aqueous medium. The catalytic efficiencies of the computationally designed mutants E115A/E188A/L362S/I270A and E115A/Y118 K/E188 V/I270A/L362S can be taken as starting points to further improve their properties towards the practical application in designing more ecology-friendly production of third-generation cephalosporins." @default.
- W3048754954 created "2020-08-18" @default.
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- W3048754954 date "2020-10-01" @default.
- W3048754954 modified "2023-10-14" @default.
- W3048754954 title "Computational design of new enzymes for hydrolysis and synthesis of third-generation cephalosporin antibiotics" @default.
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- W3048754954 doi "https://doi.org/10.1016/j.enzmictec.2020.109649" @default.
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