EC Number   |
General Information |
Reference |
|---|
    2.1.3.3 | evolution |
aOTC is a widespread enzyme that is found in a large variety of organisms from bacteria to mammals |
-, 718516 |
| 2.1.3.3 | malfunction |
absence of this enzyme impairs the growth of Listeria under mild acidic conditions at pH 4.8 and reduced its survival in synthetic human gastric fluid at pH 2.5, corresponding to a loss in ammonia production |
-, 720394 |
| 2.1.3.3 | malfunction |
inborn deficiency of OTC causes mainly urea cycle-related disorders and leads to hyperammonemic states that may become lethal. Some states of hepatotoxicity are associated woth hepatocyte disruption and release of OTC into the bloodstream |
719326 |
| 2.1.3.3 | metabolism |
anabolic ornithine transcarbamoylase is involved in the urea cycle and L-arginine biosynthesis |
-, 718516 |
| 2.1.3.3 | metabolism |
ArgF is involved in the biosynthesis of L-arginine, overview |
718678 |
| 2.1.3.3 | metabolism |
carbamoyl-phosphate synthetase and ornithine carbamoyltransferase form an efficient channeling cluster for carbamoyl phosphate, an extremely thermolabile and potentially toxic metabolic intermediate. Therefore, by physically interacting with each other, carbamoyl-phosphate synthetase and ornithine carbamoyltransferase prevent the thermodenaturation of carbamoyl phosphate in the aqueous cytoplasmic environment |
745268 |
| 2.1.3.3 | metabolism |
catabolic ornithine and putrescine carbamoyltransfer reactions constitute the second step of arginine deiminase and agmatine deiminase pathways. However, the equilibrium of in vitro carbamoyltransfer reactions is overwhelmingly towards the anabolic direction, suggesting that catabolic carbamoyltransferase is probably the limiting step of the pathways. lmo0036 is induced at the transcriptional level when Listeria monocytogenes is subjected to low-pH stress. Its expression product in Escherichia coli exhibits higher catabolic carbamoyltransfer activities under acidic conditions |
-, 720394 |
| 2.1.3.3 | metabolism |
Sulfolobus solfataricus lacks ornithine acetyltransferase and thus forms N-acetylglutamate exclusively via the energetically less favourable reaction catalysed by N-acetylglutamate synthase, investing 1 mol of acetyl CoA per mol of N-acetyl intermediate synthesized |
-, 725629 |
| 2.1.3.3 | metabolism |
the binding of carbamoyl phosphate to the enzymes aspartate and ornithine transcarbamoylase reduces the rate of thermal decomposition of carbamoyl phosphate by a factor of >5000. Both of these transcarbamoylases use an ordered-binding mechanism in which carbamoyl phosphate binds first, allowing the formation of an enzyme-carbamoyl phosphate complex. The critical step in the thermal decomposition of carbamoyl phosphate in aqueous solution, in the absence of enzyme, involves the breaking of the C-O bond facilitated by intramolecular proton transfer from the amine to the phosphate. The binding of carbamoyl phosphate to the active sites of the enzymes significantly inhibits this process by restricting the accessible conformations of the bound ligand to those disfavoring the reactive geometry |
700959 |
| 2.1.3.3 | metabolism |
the enzyme activity supports nitric oxide production in nitrergic neurons |
757570 |
