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Literature summary for 2.1.3.2 extracted from

  • Chen, P.; Van Vliet, F.; Van De Casteele, M.; Legrain, C.; Cunin, R.; Glansdorff, N.
    Aspartate transcarbamylase from the hyperthermophilic eubacterium Thermotoga maritima Fused catalytic and regulatory polypeptides form an allosteric enzyme (1998), J. Bacteriol., 180, 6389-6391 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.3.2

Activating Compound

Activating Compound Comment Organism Structure
ATP 2 mM, activates Thermotoga maritima

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli. The catalytic and regulatory functions which, in the class B ATCases from members of the Enterobacteriaceae, Vibrio sp., and archaea, are carried out by specialized polypeptides, are combined on a single type of polypeptide assembled in trimers Thermotoga maritima

Inhibitors

Inhibitors Comment Organism Structure
CTP 2 mM, about 90% inhibition Thermotoga maritima
UTP 2 mM, about 90% inhibition Thermotoga maritima

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
200000
-
 gel filtration Thermotoga maritima

Organism

Organism UniProt Comment Textmining
Thermotoga maritima P96111
-
-
Thermotoga maritima DSM 3109 P96111
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Thermotoga maritima

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
carbamoyl phosphate + L-aspartate
-
 Thermotoga maritima phosphate + N-carbamoyl-L-aspartate
-
 ?
carbamoyl phosphate + L-aspartate
-
 Thermotoga maritima DSM 3109 phosphate + N-carbamoyl-L-aspartate
-
 ?

Subunits

Subunits Comment Organism
trimer 3 * 60500, calculated from sequence Thermotoga maritima

Synonyms

Synonyms Comment Organism
aspartate transcarbamylase
-
 Thermotoga maritima
ATCase
-
 Thermotoga maritima