Article
Steady-state kinetics and isotope effects on the mutant catalytic trimer of aspartate transcarbamoylase containing the replacement of histidine 134 by alanine.
Biochemistry - 21 Jul 1992
Waldrop G L, Turnbull J L, Parmentier L E, O'Leary M H, Cleland W W, Schachman H K
Abstract excerpt
A detailed kinetic analysis of the catalytic trimer of aspartate transcarbamoylase containing the active site substitution H134A was performed to investigate the role of His 134 in the catalytic mechanism. Replacement of histidine by alanine resulted in decreases in the affinities for the two sub...
Topics
- Alanine
- Aspartate Carbamoyltransferase
- Aspartic Acid
- Binding Sites
- Carbon Isotopes
- Catalysis
- Histidine
- Hydrogen-Ion Concentration
- In Vitro Techniques
- Kinetics
- Macromolecular Substances
- Models, Molecular
- Mutation
- Phosphonoacetic Acid
- Recombinant Proteins