Article
Conserved arginine-516 of Penicillium amagasakiense glucose oxidase is essential for the efficient binding of beta-D-glucose.
The Biochemical journal - 15 Apr 2000
Witt S, Wohlfahrt G, Schomburg D, Hecht H J, Kalisz H M
Abstract excerpt
The effects of mutation of key conserved active-site residues (Tyr-73, Phe-418, Trp-430, Arg-516, Asn-518, His-520 and His-563) of glucose oxidase from Penicillium amagasakiense on substrate binding were investigated. Kinetic studies on the oxidation of beta-D-glucose combined with molecular modelling showed the side chain of Arg-516, which forms two hydrogen bonds with the 3-OH group of beta-D-glucose, to be...
Topics
- Arginine
- Binding Sites
- Catalysis
- Circular Dichroism
- Conserved Sequence
- Escherichia coli
- Glucose
- Glucose Oxidase
- Hydrogen Bonding
- Kinetics
- Models, Molecular
- Mutation
- Penicillium
- Protein Binding
- Protein Conformation
- Recombinant Proteins