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Literature summary for 2.1.3.2 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
Search for more literature for 2.1.3.2

Activating Compound

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

Cloned(Commentary)

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

Inhibitors

Inhibitors Comment Organism Structure
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
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
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
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]

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Sulfolobus acidocaldarius
-
-
-
Sulfolobus acidocaldarius Q55338 catalytic subunit PyrB
-

Purification (Commentary)

Purification (Comment) Organism
-
 Sulfolobus acidocaldarius

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

Temperature Stability [°C]

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