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Article

Saturation mutagenesis reveals that GLU54 of norovirus 3C-like protease is not essential for the proteolytic activity.

Journal of biochemistry - 1 Dec 2008

Someya Yuichi, Takeda Naokazu, Wakita Takaji

Abstract excerpt

The norovirus 3C-like protease is a member of the chymotrypsin-like serine protease superfamily. Previous characterization of its crystal structure has implicated the Glu54-His30-Cys139 triad in the catalysis. In the present study, the Glu54 residue of the protease was subjected to site-saturation mutagenesis, with the result that nearly half of the mutants retained the significant proteolytic activity. It was...

Topics

3C Viral Proteases
Catalysis
Cysteine Endopeptidases
Glutamic Acid
Models, Genetic
Mutagenesis, Site-Directed
Mutation
Norovirus
Protein Processing, Post-Translational
Substrate Specificity
Viral Proteins

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Identifiers

PMID: 18838436
DOI: 10.1093/jb/mvn130
PMCID: PMC7109903

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