Structure-based design of a lysozyme with altered catalytic activity.

doi:10.1038/nsb1195-1007

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Article

Structure-based design of a lysozyme with altered catalytic activity.

Nature structural biology - 1 Nov 1995

Kuroki R, Weaver L H, Matthews B W

Abstract excerpt

Here we show that the substitution Thr 26-->His in the active site of T4 lysozyme causes the product to change from the alpha- to the beta-anomer. This implies an alteration in the catalytic mechanism of the enzyme. From the change in product, together with inspection of relevant crystal structur...

Topics

Animals
Binding Sites
Biological Evolution
Carbohydrate Sequence
Catalysis
Crystallography
Egg White
Glycoside Hydrolases
Hydrolysis
Models, Molecular
Molecular Sequence Data
Muramidase
Mutation
Protein Engineering
Stereoisomerism
Structure-Activity Relationship

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