Article
The tryptophan synthase alpha 2 beta 2 complex: kinetic studies with a mutant enzyme (beta K87T) to provide evidence for allosteric activation by an aminoacrylate intermediate.
Biochemistry - 3 Oct 1995
Banik U, Zhu D M, Chock P B, Miles E W
Abstract excerpt
To investigate the mechanism by which the tryptophan synthase beta subunit accelerates the cleavage of the indole-3-glycerol phosphate catalyzed by the alpha subunit (alpha reaction), kinetic experiments were carried out with wild-type and mutant forms of the alpha 2 beta 2 complex. Previous studies indicate that this activation can be attributed to the conformational changes associated with the formation of a...
Topics
- Acrylates
- Allosteric Regulation
- Enzyme Activation
- Hydrolysis
- Kinetics
- Mutation
- Tryptophan Synthase
