Article
Enzymatic properties of the cysteinesulfinic acid derivative of the catalytic-base mutant Glu400-->Cys of glucoamylase from Aspergillus awamori.
Biochemistry - 17 Mar 1998
Fierobe H P, Clarke A J, Tull D, Svensson B
Abstract excerpt
The pKa of the catalytic base was lowered and its distance to the general acid catalyst, Glu179, was increased in the glucoamylase from Aspergillus awamori by replacing the catalytic base Glu400 with cysteine followed by oxidation to cysteinesulfinic acid [Fierobe, H.-P., Mirgorodskaya, E., McGui...
Topics
- 1-Deoxynojirimycin
- Acarbose
- Amino Acid Substitution
- Amino Sugars
- Aspergillus
- Binding, Competitive
- Catalysis
- Cysteine
- Enzyme Activation
- Glucan 1,4-alpha-Glucosidase
- Glucose
- Glutamic Acid
- Hydro-Lyases
- Hydrogen-Ion Concentration
- Hydrolysis
- Isomaltose
- Kinetics
- Magnetic Resonance Spectroscopy