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Literature summary extracted from

  • Durbecq, V.; Thia-Toong, T.L.; Charlier, D.; Villeret, V.; Roovers, M.; Wattiez, R.; Legrain, C.; Glansdorff, N.
    Aspartate carbamoyltransferase from the thermoacidophilic archaeon Sulfolobus acidocaldarius cloning, sequence analysis, enzyme purification and characterization (1999), Eur. J. Biochem., 264, 233-241.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.1.3.2 ATP holoenzyme, catalytic subunits alone are inhibited Sulfolobus acidocaldarius
2.1.3.2 CTP holoenzyme, catalytic subunits alone are inhibited Sulfolobus acidocaldarius
2.1.3.2 GTP holoenzyme, catalytic subunits alone are inhibited Sulfolobus acidocaldarius
2.1.3.2 UTP holoenzyme, catalytic subunits alone are inhibited Sulfolobus acidocaldarius

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.3.2
-
 Sulfolobus acidocaldarius
2.1.3.2 expression in Escherichia coli Sulfolobus acidocaldarius

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.3.2 ATP inhibitory effect on the catalytic subunits encoded by the sole pyrB gene. The complete ATCase purified from recombinant Escherichia coli is strongly activated Sulfolobus acidocaldarius
2.1.3.2 CTP inhibitory effect on the catalytic subunits encoded by the sole pyrB gene. The complete ATCase purified from recombinant Escherichia coli is strongly activated Sulfolobus acidocaldarius
2.1.3.2 GTP inhibitory effect on the catalytic subunits encoded by the sole pyrB gene. The complete ATCase purified from recombinant Escherichia coli is strongly activated Sulfolobus acidocaldarius
2.1.3.2 UTP inhibitory effect on the catalytic subunits encoded by the sole pyrB gene. The complete ATCase purified from recombinant Escherichia coli is strongly activated Sulfolobus acidocaldarius

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.3.2 additional information
-
 additional information sigmoidal saturation curve for aspartate Sulfolobus acidocaldarius
2.1.3.2 0.2
-
 Carbamoyl phosphate holoenzyme Sulfolobus acidocaldarius
2.1.3.2 0.6
-
 Carbamoyl phosphate catalytic subunits Sulfolobus acidocaldarius

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.3.2 18000
-
 6 * 36500 + 6 * 18000, SDS-PAGE Sulfolobus acidocaldarius
2.1.3.2 36500
-
 6 * 36500 + 6 * 18000, SDS-PAGE Sulfolobus acidocaldarius
2.1.3.2 340000
-
 gel filtration Sulfolobus acidocaldarius
2.1.3.2 340000
-
 holoenzyme, gel filtration Sulfolobus acidocaldarius

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 Sulfolobus acidocaldarius
-
 phosphate + N-carbamoyl-L-aspartate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.2 Sulfolobus acidocaldarius
-
-
-
2.1.3.2 Sulfolobus acidocaldarius Q55338 catalytic subunit PyrB
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.3.2
-
 Sulfolobus acidocaldarius

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.3.2 29.95
-
 at 55°C Sulfolobus acidocaldarius

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
2.1.3.2 dodecamer 6 * 36500 + 6 * 18000, SDS-PAGE Sulfolobus acidocaldarius

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.1.3.2 85
-
 no loss of activity after 15 min Sulfolobus acidocaldarius
2.1.3.2 90
-
 native and recombinant enzyme, loss of less than 10% activity after 40 min Sulfolobus acidocaldarius