Mechanistic consequences of mutation of the active site nucleophile Glu 358 in Agrobacterium beta-glucosidase.

@article{Withers1992MechanisticCO,
  title={Mechanistic consequences of mutation of the active site nucleophile Glu 358 in Agrobacterium beta-glucosidase.},
  author={Stephen G Withers and Karen Rupitz and D E Trimbur and Richard A. Warren},
  journal={Biochemistry},
  year={1992},
  volume={31 41},
  pages={9979-85}
}
The replacement of the active site nucleophile Glu 358 in Agrobacterium beta-glucosidase by Asn and Gln by site-directed mutagenesis results in essentially complete inactivation of the enzyme, while replacement by Asp generates a mutant with a rate constant for the first step, formation of the glycosylenzyme, some 2500 times lower than that of the native enzyme. This low activity is shown to be a true property of the mutant and not due to contaminating wild-type enzyme by active site titration… CONTINUE READING

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