Article
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzyme.
Biochemistry - 1 Mar 1994
Bohren K M, Grimshaw C E, Lai C J, Harrison D H, Ringe D, Petsko G A, Gabbay K H
Abstract excerpt
The active site of human aldose reductase contains two residues, His110 and Tyr48, either of which could be the proton donor during catalysis. Tyr48 is a candidate since its hydroxyl group is in proximity to Lys77 and thus may have an abnormally low pKa value. To distinguish between these possibi...
Topics
- Aldehyde Reductase
- Base Sequence
- Citrates
- Citric Acid
- Computer Graphics
- Crystallography, X-Ray
- DNA Primers
- Histidine
- Humans
- Hydrogen-Ion Concentration
- Kinetics
- Models, Molecular
- Molecular Sequence Data
- Mutation