Literature summary for 2.1.3.2 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.

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Activating Compound

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

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

Organism

Organism	UniProt	Comment	Textmining
Moritella profunda	-	-	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
ATCase	-	Moritella profunda

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Release 2023.1 (January 2023)