Literature summary for 2.1.3.3 extracted from

Tricot, C.; Villeret, V.; Sainz, G.; Dideberg, O.; Stalon, V.
Allosteric regulation in Pseudomonas aeruginosa catabolic ornithine carbamoyltransferase revisited: association of concerted homotropic cooperative interactions and local heterotropic effects (1998), J. Mol. Biol., 283, 695-704.

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Activating Compound

Activating Compound	Comment	Organism	Structure
AMP	-	Pseudomonas aeruginosa
arsenate	potent activator in the concentration range of 0-10 mM	Pseudomonas aeruginosa
phosphate	potent activator in the concentration range of 0-10 mM	Pseudomonas aeruginosa

Protein Variants

Protein Variants	Comment	Organism
E105G	no cooperativity towards carbamoyl phosphate, follows Michaelis-Menten kinetics	Pseudomonas aeruginosa

Inhibitors

Inhibitors	Comment	Organism	Structure
spermidine	E105G mutant enzyme, competitive vs. carbamoylphosphate	Pseudomonas aeruginosa

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	-	catabolic ornithine carbamoyltransferase	-

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Release 2023.1 (January 2023)