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Literature summary extracted from

  • Van Boxstael, S.; Cunin, R.; Khan, S.; Maes, D.
    Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi: thermostability and 1.8 A resolution crystal structure of the catalytic subunit complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate (2003), J. Mol. Biol., 326, 203-216.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.3.2 expression of catalytic subunit in Escherichia coli Pyrococcus abyssi

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.3.2 hanging-drop vapour-diffusion, 0.002 ml of enzyme solution, 7 mg/ml, in 20 mM Tris-HCl, pH 8.2, 2 mM 2-mercaptoethanol, 300 mM NaCl, is mixed with 0.002 ml reservoir solution consisting of 1.4 M citrate, pH 6.8, X-ray structure to 1.8 A resolution Pyrococcus abyssi

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.3.2 N-(Phosphonoacetyl)-L-aspartate 0.002 mM, 50% inhibition of catalytic subunit Pyrococcus abyssi

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.3.2 0.038
-
Carbamoyl phosphate recombinant catalytic subunit, at 37°C Pyrococcus abyssi
2.1.3.2 12.3
-
L-aspartate recombinant catalytic subunit, at 30°C Pyrococcus abyssi
2.1.3.2 14.1
-
L-aspartate recombinant catalytic subunit, at 45°C Pyrococcus abyssi
2.1.3.2 15.5
-
L-aspartate recombinant catalytic subunit, at 37°C Pyrococcus abyssi
2.1.3.2 19.7
-
L-aspartate recombinant catalytic subunit, at 55°C Pyrococcus abyssi

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 Pyrococcus abyssi
-
phosphate + N-carbamoyl-L-aspartate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.2 Pyrococcus abyssi P77918
-
-

Substrates and Products (Substrate)

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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.1.3.2 90
-
catalytic subunit, half-life: 80 min, half-life of holenzyme: 240 min Pyrococcus abyssi
2.1.3.2 98
-
half-life of the holoenzyme is 2.5 times higher than that of the catalytic subunit Pyrococcus abyssi