Article
Identification of an active-site residue in yeast invertase by affinity labeling and site-directed mutagenesis.
The Journal of biological chemistry - 5 Jul 1990
Reddy V A, Maley F
Abstract excerpt
Deglycosylated yeast invertase is irreversibly inactivated by conduritol B epoxide (CBE), an active-site-directed reagent. The inactivated enzyme contained 0.8 mol of CBE/mol of invertase monomer suggesting that the inactivation results from the modification of a single amino acid residue. Peptic...
Topics
- Acetylglucosaminidase
- Affinity Labels
- Amino Acid Sequence
- Aspartic Acid
- Base Sequence
- Binding Sites
- Catalysis
- Chromatography, High Pressure Liquid
- Glycoside Hydrolases
- Glycosylation
- Inositol
- Kinetics
- Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
- Molecular Sequence Data
- Mutation
- Peptide Fragments
- Saccharomyces cerevisiae
- Trypsin