Literature summary for 6.3.5.5 extracted from

Guy, H.I.; Evans, D.R.
Trapping an activated conformation of mammalian carbamylphosphate synthetase (1997), J. Biol. Chem., 272, 19906-19912.

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Protein Variants

Protein Variants	Comment	Organism
additional information	the 29-amino acid linker, which connects the glutaminase domain and the synthetase domain is deleted. The deletion mutant catalyzes glutamine-dependent carbamoyl phosphate synthesis, but is activated 10fold relative to its wild type counterpart. NH4+-dependent synthesis of carbamoyl phosphate is abolished. The mutant enzyme is still sensitive to inhibition by the allosteric effector UTP, but is no longer activated by the allosteric effector phosphoribosyl diphosphate. The linker appears to serve as a spacer that allows the complex to cycle between two conformations, an open low activity form in which the NH4+ site on the synthetase domain is accessible and an activated conformation in which the NH4+ generated in situ from Gln is directly channeled to the synthetase domain active site and access to exogenous NH4+ is blocked	Mammalia

Organism

Organism	UniProt	Comment	Textmining
Mammalia	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2 ATP + L-Gln + HCO3-	-	Mammalia	2 ADP + phosphate + L-Glu + carbamoyl phosphate	-	?

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Release 2023.1 (January 2023)