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Literature summary for 2.1.3.2 extracted from

  • Grayson, D.R.; Evans, D.R.
    The isolation and characterization of the aspartate transcarbamylase domain of the multifunctional protein, CAD (1983), J. Biol. Chem., 258, 4123-4129.
    View publication on PubMed

General Stability

General Stability Organism
dimethylsulfoxid and glycerol are required to stabilize the enzyme Mesocricetus auratus

Inhibitors

Inhibitors Comment Organism Structure
aspartate at high concentrations Mesocricetus auratus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.009
-
L-aspartate multienzyme complex Mesocricetus auratus
0.02
-
Carbamoyl phosphate multienzyme complex and aspartate transcarbamoylase activity domain of the multienzyme complex alone Mesocricetus auratus
0.0207
-
Carbamoyl phosphate
-
Mesocricetus auratus
0.021
-
L-aspartate aspartate transcarbamoylase activity domain of the multienzyme complex alone Mesocricetus auratus
0.02134
-
L-aspartate
-
Mesocricetus auratus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
hamster aspartate carbamoyltransferase domain is an oligomer consisting of 2 or 3 identical copies of the 40000 Da proteolytic fragment of CAD, 2 or 3 * 40000, SDS-PAGE Mesocricetus auratus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
carbamoylphosphate + L-aspartate Mesocricetus auratus
-
phosphate + N-carbamoyl-L-aspartate
-
?

Organism

Organism UniProt Comment Textmining
Mesocricetus auratus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
aspartate transcarbamoylase activity domain of the multienzyme complex Mesocricetus auratus

Source Tissue

Source Tissue Comment Organism Textmining
cell culture simian virus 40 transformed syrian hamster cell line Mesocricetus auratus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
carbamoyl phosphate + L-aspartate
-
Mesocricetus auratus phosphate + N-carbamoyl-L-aspartate
-
?
carbamoylphosphate + L-aspartate
-
Mesocricetus auratus phosphate + N-carbamoyl-L-aspartate
-
?

Subunits

Subunits Comment Organism
More hamster aspartate carbamoyltransferase domain is an oligomer consisting of 2 or 3 identical copies of the 40000 Da proteolytic fragment of CAD, 2 or 3 * 40000, SDS-PAGE Mesocricetus auratus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
35.9
-
Carbamoyl phosphate aspartate transcarbamoylase activity domain of the multienzyme complex Mesocricetus auratus
57.4
-
Carbamoylphosphate multienzyme complex Mesocricetus auratus
79.7
-
aspartate aspartate transcarbamoylase activity domain of the multienzyme complex Mesocricetus auratus
156
-
L-aspartate multienzyme complex Mesocricetus auratus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.59
-
L-aspartate aspartate transcarbamoylase activity domain of the multienzyme complex Mesocricetus auratus
13.56
-
L-aspartate multienzyme complex Mesocricetus auratus