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Literature summary extracted from

  • De Vos, D.; Xu, Y.; Hulpiau, P.; Vergauwen, B.; Van Beeumen, J.J.
    Structural investigation of cold activity and regulation of aspartate carbamoyltransferase from the extreme psychrophilic bacterium Moritella profunda (2007), J. Mol. Biol., 365, 379-395.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.1.3.2 ATP dual regulatory pattern, activating the enzyme at low concentrations and inhibiting it in the mM range Moritella profunda

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.3.2 the crystal structure of the unliganded Moritella profunda ATCase shows resemblance to a more extreme T state reported previously for an Escherichia coli ATCase mutant Moritella profunda

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.3.2 ATP dual regulatory pattern, activating the enzyme at low concentrations and inhibiting it in the mM range Moritella profunda
2.1.3.2 CTP
-
 Moritella profunda
2.1.3.2 UTP
-
 Moritella profunda

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.2 Moritella profunda
-
-
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
2.1.3.2 ATCase
-
 Moritella profunda