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Literature summary 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

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.3.2 aspartate at high concentrations Mesocricetus auratus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.3.2 0.009
-
 L-aspartate multienzyme complex Mesocricetus auratus
2.1.3.2 0.02
-
 Carbamoyl phosphate multienzyme complex and aspartate transcarbamoylase activity domain of the multienzyme complex alone Mesocricetus auratus
2.1.3.2 0.0207
-
 Carbamoyl phosphate
-
 Mesocricetus auratus
2.1.3.2 0.021
-
 L-aspartate aspartate transcarbamoylase activity domain of the multienzyme complex alone Mesocricetus auratus
2.1.3.2 0.02134
-
 L-aspartate
-
 Mesocricetus auratus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.3.2 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)

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

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.2 Mesocricetus auratus
-
-
-

Purification (Commentary)

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

Source Tissue

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

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
2.1.3.2 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]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.3.2 35.9
-
 Carbamoyl phosphate aspartate transcarbamoylase activity domain of the multienzyme complex Mesocricetus auratus
2.1.3.2 57.4
-
 Carbamoylphosphate multienzyme complex Mesocricetus auratus
2.1.3.2 79.7
-
 aspartate aspartate transcarbamoylase activity domain of the multienzyme complex Mesocricetus auratus
2.1.3.2 156
-
 L-aspartate multienzyme complex Mesocricetus auratus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.1.3.2 4.59
-
 L-aspartate aspartate transcarbamoylase activity domain of the multienzyme complex Mesocricetus auratus
2.1.3.2 13.56
-
 L-aspartate multienzyme complex Mesocricetus auratus