Inhibitors | Comment | Organism | Structure |
---|---|---|---|
N-phosphonacetyl-L-aspartate | binding of the bisubstrate analogue N-phosphonacetyl-L-aspartate to the aspartate transcarbamoylase subunit inhibits the activity of the distal dihydroorotase subunit | Aquifex aeolicus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics | Aquifex aeolicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
carbamoyl phosphate + L-aspartate | Aquifex aeolicus | - |
phosphate + N-carbamoyl-L-aspartate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aquifex aeolicus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
carbamoyl phosphate + L-aspartate | - |
Aquifex aeolicus | phosphate + N-carbamoyl-L-aspartate | - |
? |
Subunits | Comment | Organism |
---|---|---|
dodecamer | CAD enzyme complex including the aspartate transcarbamoylase. The Aquifex aeolicus DHO-ATC dodecameric complex consists of two trimeric ATC subunits and three DHO dimers. ATC is a trimer consisting of a carbamoyl phosphate binding domain and an aspartate binding domain | Aquifex aeolicus |
Synonyms | Comment | Organism |
---|---|---|
aspartate transcarbamoylase | - |
Aquifex aeolicus |
ATC | - |
Aquifex aeolicus |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.000000621 | - |
N-phosphonacetyl-L-aspartate | pH and temperature not specified in the publication | Aquifex aeolicus |
General Information | Comment | Organism |
---|---|---|
metabolism | aspartate transcarbamoylase and dihydroorotase, enzymes that catalyze the second and third step in de novo pyrimidine biosynthesis, are associated in dodecameric complexes in Aquifex aeolicus and many other organisms, intersubunit communication in the dihydroorotase-aspartate transcarbamoylase complex of Aquifex aeolicus, overview. The architecture of the dodecamer is ideally suited to channel the intermediate, carbamoyl aspartate from its site of synthesis on the ATC subunit to the active site of dihydroorotase, which catalyzes the next step in the pathway, because both reactions occur within a large, internal solvent-filled cavity. The apparent second-order rate constant (kcat/Km) of ATC is 7.0fold greater than that of dihydroorotase | Aquifex aeolicus |
additional information | the dihydroorotase loop A that binds between the two ATC domains is an allosteric or noncompletive ATC inhibitor with Ki 5 of 0.022 mM, loop A is an important component of the functional linkage between the enzymes. modeling, overview | Aquifex aeolicus |