Article
A model for oxidative modification of glutamine synthetase, based on crystal structures of mutant H269N and the oxidized enzyme.
Biochemistry - 10 Aug 1993
Liaw S H, Villafranca J J, Eisenberg D
Abstract excerpt
Proteolytic degradation of glutamine synthetase (GS) in Escherichia coli is known to follow "marking" by oxidative modification. At an early stage of the degradative pathway, oxidation of His 269 and Arg 344 abolishes GS enzymatic activity. We propose a mechanism for the early stage of oxidative inactivation of GS on the basis of the crystal structure of H269N and tryptophan fluorescence spectra of H269N and...
Topics
- Binding Sites
- Escherichia coli
- Glutamate-Ammonia Ligase
- Metals
- Models, Molecular
- Mutation
- Oxidation-Reduction
- Protein Conformation
- Recombinant Proteins
- Salmonella typhimurium
- Spectrometry, Fluorescence