Article
Biosynthetic thiolase from Zoogloea ramigera. Evidence for a mechanism involving Cys-378 as the active site base.
The Journal of biological chemistry - 5 May 1991
Palmer M A, Differding E, Gamboni R, Williams S F, Peoples O P, Walsh C T, Sinskey A J, Masamune S
Abstract excerpt
Biosynthetic thiolase from Zoogloea ramigera was inactivated with a mechanism-based inactivator, 3-pentynoyl-S-pantetheine-11-pivalate (3-pentynoyl-SPP) where K1 = 1.25 mM and kinact = 0.26 min-1, 2,3-pentadienoyl-SPP obtained from nonenzymatic rearrangement of 3-pentynoyl-SPP where K1 = 1.54 mM...
Topics
- Acetyl-CoA C-Acetyltransferase
- Acrylates
- Affinity Labels
- Alkynes
- Amino Acid Sequence
- Binding Sites
- Catalysis
- Cysteine
- Kinetics
- Molecular Sequence Data
- Mutation
- Pantetheine
- Protons
- Sequence Homology, Nucleic Acid
- Substrate Specificity
- Zoogloea