Literature summary for 6.3.4.2 extracted from

Lewis, D.A.; Villafranca, J.J.
Investigation of the mechanism of CTP synthetase using rapid quench and isotope partitioning methods (1989), Biochemistry, 28, 8454-8459.

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KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.027	-	UTP	pH 8.0, 25°C, without GTP	Escherichia coli
0.054	-	ATP	pH 8.0, 25°C, without GTP	Escherichia coli
0.071	-	UTP	pH 8.0, 25°C, activation with GTP	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	harboring the plasmid pMW5	-

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate	mechanism, the initial chemical step catalyzed by CTP synthetase is the phosphorylation of UTP by ATP to form an enzyme-bound intermediate	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + UTP + glutamine	-	Escherichia coli	ADP + phosphate + CTP + Glu	-	?
ATP + UTP + NH4+	-	Escherichia coli	ADP + phosphate + CTP	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	-	Escherichia coli

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Release 2023.1 (January 2023)