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Increased Activity of β-glucuronidase Variants Produced by Site-Directed Mutagenesis

Increased Activity of β-glucuronidase Variants Produced by Site-Directed Mutagenesis

Xiaolei Zhang, Pongkwan Sitasuwan, Gary Horvath, Jia Yang, Yuzhe Nie, Margarita Marinova, L Andrew Lee, Qian Wang

Enzyme Microb Technol. 2018 Feb;109:20-24.

PMID: 29224622

Abstract:

β-glucuronidase (BGus) is an essential glycosyl hydrolase which has been widely used in biological and biomedical applications. In this paper, we report the construction and screening of nineteen Escherichia coli BGus (EBGus) mutants using site-directed mutagenesis. The mutants G559N, G559S and G559T showed a 3-5 fold increase in enzyme activity in comparison to wild type EBGus. In particular, G559S, with the highest activity, showed 2-6 fold enhanced activity compared to abalone and snail BGus extracts. Moreover, the glycine to serine mutagenesis for the same site in Staphylococcus sp. RLH1 BGus (StBGus) exhibited significantly enhanced activity, which indicated the importance of the G559→S mutation on BGus function. Based on this structural analysis, we postulate that the mutation at G559 plays an important role in the stabilization of the enzyme conformation, and thereby facilitates the effective binding of substrate.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR424866	β-Glucuronidase from abalone			Price

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