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Site-directedmutagenesis was used to investigate the controlof 2-oxoacid cosubstrate selectivity by deacetoxycephalo-sporin C synthase. The wild-type enzyme has a requirementfor 2-oxoglutarate and cannot efficiently use hydrophobic2-oxoacids (e.g. 2-oxohexanoic acid, 2-oxo-4-methyl-penta-noic acid) as the cosubstrate. The followingmutant enzymeswere produced: R258A, R258L, R258F, R258H andR258K. All of the mutants have broadened cosubstrateselectivity and were able to utilize hydrophobic 2-oxoacids.The efficiency of 2-oxoglutarate utilization by all mutantswas decreased as compared to the wild-type enzyme, andin some cases activity was abolished with the naturalcosubstrate....
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: The kinetic properties of various R258 mutants of deacetoxycephalosporin C synthase
