Article
Steady-state kinetics and analysis of pH dependence on wild-type and a modified allosteric Pseudomonas aeruginosa ornithine carbamoyltransferase containing the replacement of glutamate 105 by alanine.
European journal of biochemistry - 1 Aug 1993
Tricot C, Nguyen V T, Stalon V
Abstract excerpt
The substitution of alanine for glutamate at position 105 (E105A) of the allosteric ornithine carbamoyltransferase (OTCase) of Pseudomonas aeruginosa abolishes the carbamoylphosphate (CP) cooperativity observed in the wild-type enzyme. A kinetic analysis of [E105A]OTCase was performed in order to...
Topics
- Alanine
- Allosteric Regulation
- Glutamates
- Glutamic Acid
- Hydrogen-Ion Concentration
- Kinetics
- Mutation
- Ornithine Carbamoyltransferase
- Pseudomonas aeruginosa
- Substrate Specificity