Article
Abnormally high pKa of an active-site glutamic acid residue in Bacillus circulans xylanase. The role of electrostatic interactions.
European journal of biochemistry - 15 Sept 1995
Davoodi J, Wakarchuk W W, Campbell R L, Carey P R, Surewicz W K
Abstract excerpt
The active site of Bacillus circulans xylanase (1,4-beta-D-xylanohydrolase, EC 3.2.1.8) contains two glutamic acid residues, Glu78 and Glu172, which are crucial for the catalytic activity of the enzyme. Fourier-transform infrared spectroscopy was used to determine the ionization state of these re...
Topics
- Anions
- Bacillus
- Binding Sites
- Calorimetry, Differential Scanning
- Circular Dichroism
- Endo-1,4-beta Xylanases
- Enzyme Stability
- Glutamic Acid
- Hot Temperature
- Hydrogen-Ion Concentration
- Models, Molecular