Article
Allosteric regulation in Pseudomonas aeruginosa catabolic ornithine carbamoyltransferase revisited: association of concerted homotropic cooperative interactions and local heterotropic effects.
Journal of molecular biology - 30 Oct 1998
Tricot C, Villeret V, Sainz G, Dideberg O, Stalon V
Abstract excerpt
The allosteric catabolic ornithine carbamoyltransferase (OTCase) from Pseudomonas aeruginosa, a dodecamer build up of four trimers of identical subunits, shows strong carbamoylphosphate homotropic co-operativity. Its activity is allosterically inhibited by spermidine and activated by AMP. Modifie...
Topics
- Adenosine Monophosphate
- Allosteric Regulation
- Amino Acid Sequence
- Arsenates
- Bacterial Proteins
- Binding, Competitive
- Diphosphates
- Enzyme Activation
- Enzyme Repression
- Escherichia coli Proteins
- Kinetics
- Membrane Proteins
- Models, Molecular
- Molecular Sequence Data