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Literature summary extracted from

  • Purcarea, C.; Evans, D.R.; Herve, G.
    Channeling of carbamoyl phosphate to the pyrimidine and arginine biosynthetic pathways in the deep sea hyperthermophilic archaeon Pyrococcus abyssi (1999), J. Biol. Chem., 274, 6122-6129.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.3.2 N-(phosphonacetyl)-L-aspartate there is no preferential partitioning of carbamoyl phosphate between the arginine and pyrimidine biosynthetic pathways. Channeling must occur during the dynamic association of coupled enzymes pairs. The interaction of carbamoyl-phosphate synthetase/aspartate transcarbamoylase is demonstrated by the unexpectedly weak inhibition of the coupled reaction by the bisubstrate analog, N-(phosphonacetyl)-L-aspartate Pyrococcus abyssi
6.3.5.5 N-(phosphonacetyl)-L-aspartate there is no preferential partitioning of carbamoyl phosphate between the arginine and pyrimidine biosynthetic pathways. Channeling must occur during the dynamic association of coupled enzymes pairs. The interaction of carbamoyl-phosphate synthetase/aspartate transcarbamoylase is demonstrated by the unexpectedly weak inhibition of the coupled reaction by the bisubstrate analog, N-(phosphonacetyl)-L-aspartate Pyrococcus abyssi

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.3.3 0.008
-
 Carbamoyl phosphate pH 8.0, 37°C Pyrococcus abyssi
2.1.3.3 0.0285
-
 L-ornithine pH 8.0, 37°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 carbamoyl phosphate + L-aspartate Pyrococcus abyssi there is no preferential partitioning of carbamoyl phosphate between the arginine and pyrimidine biosynthetic pathways. Channeling must occur during the dynamic association of coupled enzymes pairs. The interaction of carbamoyl-phosphate synthetase/aspartate transcarbamoylase is demonstrated by the unexpectedly weak inhibition of the coupled reaction by the bisubstrate analog, N-(phosphonacetyl)-L-aspartate. In the coupled reaction, the effective concentration of carbamoyl phosphate in the vicinity of the aspartate transcarbamoylase active site is 96fold higher than the concentration in the bulk phase. Channeling probably plays an essential role in protecting this very unstable intermediate of metabolic pathways performing at extreme temperatures phosphate + N-carbamoyl-L-aspartate
-
 ?
2.1.3.3 carbamoyl phosphate + L-ornithine Pyrococcus abyssi there is no preferential partitioning of carbamoyl phosphate between the arginine and pyrimidine biosynthetic pathways. Channeling must occur during the dynamic association of coupled enzymes pairs phosphate + L-citrulline
-
 ?
6.3.5.5 ATP + L-glutamine + HCO3- + H2O Pyrococcus abyssi there is no preferential partitioning of carbamoyl phosphate between the arginine and pyrimidine biosynthetic pathways. Channeling must occur during the dynamic association of coupled enzymes pairs. The interaction of carbamoyl-phosphate synthetase/aspartate transcarbamoylase is demonstrated by the unexpectedly weak inhibition of the coupled reaction by the bisubstrate analog, N-(phosphonacetyl)-L-aspartate. In the coupled reaction, the effective concentration of carbamoyl phosphate in the vicinity of the aspartate transcarbamoylase active site is 96fold higher than the concentration in the bulk phase. Channeling probably plays an essential role in protecting this very unstable intermediate of metabolic pathways performing at extreme temperatures 2 ADP + phosphate + L-glutamate + carbamoyl phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.2 Pyrococcus abyssi P77918
-
-
2.1.3.3 Pyrococcus abyssi O93656
-
-
6.3.5.5 Pyrococcus abyssi
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.3.2 carbamoyl phosphate + L-aspartate there is no preferential partitioning of carbamoyl phosphate between the arginine and pyrimidine biosynthetic pathways. Channeling must occur during the dynamic association of coupled enzymes pairs. The interaction of carbamoyl-phosphate synthetase/aspartate transcarbamoylase is demonstrated by the unexpectedly weak inhibition of the coupled reaction by the bisubstrate analog, N-(phosphonacetyl)-L-aspartate. In the coupled reaction, the effective concentration of carbamoyl phosphate in the vicinity of the aspartate transcarbamoylase active site is 96fold higher than the concentration in the bulk phase. Channeling probably plays an essential role in protecting this very unstable intermediate of metabolic pathways performing at extreme temperatures Pyrococcus abyssi phosphate + N-carbamoyl-L-aspartate
-
 ?
2.1.3.3 carbamoyl phosphate + L-ornithine there is no preferential partitioning of carbamoyl phosphate between the arginine and pyrimidine biosynthetic pathways. Channeling must occur during the dynamic association of coupled enzymes pairs Pyrococcus abyssi phosphate + L-citrulline
-
 ?
6.3.5.5 ATP + L-glutamine + HCO3- + H2O there is no preferential partitioning of carbamoyl phosphate between the arginine and pyrimidine biosynthetic pathways. Channeling must occur during the dynamic association of coupled enzymes pairs. The interaction of carbamoyl-phosphate synthetase/aspartate transcarbamoylase is demonstrated by the unexpectedly weak inhibition of the coupled reaction by the bisubstrate analog, N-(phosphonacetyl)-L-aspartate. In the coupled reaction, the effective concentration of carbamoyl phosphate in the vicinity of the aspartate transcarbamoylase active site is 96fold higher than the concentration in the bulk phase. Channeling probably plays an essential role in protecting this very unstable intermediate of metabolic pathways performing at extreme temperatures Pyrococcus abyssi 2 ADP + phosphate + L-glutamate + carbamoyl phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.3.2 ATCase
-
 Pyrococcus abyssi
2.1.3.3 otcase
-
 Pyrococcus abyssi
6.3.5.5 carbamoyl-phosphate synthetase
-
 Pyrococcus abyssi
6.3.5.5 CPSase
-
 Pyrococcus abyssi

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.3.3 37
-
 assay at Pyrococcus abyssi
6.3.5.5 37
-
 assay at Pyrococcus abyssi

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.3.3 8
-
 assay at Pyrococcus abyssi