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Literature summary for 2.1.3.2 extracted from

  • Evans, H.G.; Fernando, R.; Vaishnav, A.; Kotichukkala, M.; Heyl, D.; Hachem, F.; Brunzelle, J.S.; Edwards, B.F.; Evans, D.R.
    Intersubunit communication in the dihydroorotase-aspartate transcarbamoylase complex of Aquifex aeolicus (2014), Protein Sci., 23, 100-109.
    View publication on PubMedView publication on EuropePMC

Inhibitors

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 [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics Aquifex aeolicus

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Aquifex aeolicus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
carbamoyl phosphate + L-aspartate
-
Aquifex aeolicus phosphate + N-carbamoyl-L-aspartate
-
?

Subunits

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

Synonyms Comment Organism
aspartate transcarbamoylase
-
Aquifex aeolicus
ATC
-
Aquifex aeolicus

Ki Value [mM]

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

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