Literature summary for 2.7.7.15 extracted from

Yang, W.; Boggs, K.P.; Jackowski, S.
The association of lipid activators with the amphipathic helical domain of CTP:phosphocholine cytidylyltransferase accelerates catalysis by increasing the affinity of the enzyme for CTP (1995), J. Biol. Chem., 270, 23951-23957.

Search for more literature for 2.7.7.15

Cloned(Commentary)

Cloned (Comment)	Organism
wild-type and deletion mutants delta312-367, delta231-367 and delta257-367	Rattus norvegicus

Protein Variants

Protein Variants	Comment	Organism
additional information	DELTA delta257-367 exhibits significantly lower specific activity and can not be activated by lipid, deletion mutant DELTA231-367 can not be activated by lipid	Rattus norvegicus

Inhibitors

Inhibitors	Comment	Organism	Structure
1-O-octadecyl-2-O-methyl-rac-glycero-3-phosphatidylcholine	ET-18-OCH3, non-hydrolyzable lysophosphatidylcholine analog, competitive with respect to the lipid activator	Rattus norvegicus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.5	-	CTP	delta312-367 mutant, presence of lipid, pH 6.5, 37°C	Rattus norvegicus
0.7	-	CTP	wild-type, presence of lipid, pH 6.5, 37°C	Rattus norvegicus
13.2	-	CTP	DELTA257-367 mutant, pH 6.5, 37°C	Rattus norvegicus
13.9	-	CTP	DELTA312-367 mutant, absence of lipid, pH 6.5, 37°C	Rattus norvegicus
19.2	-	CTP	DELTA231-367 mutant, pH 6.5, 37°C	Rattus norvegicus
24.7	-	CTP	wild-type, absence of lipid, pH 6.5, 37°C	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
CTP + choline phosphate	-	Rattus norvegicus	diphosphate + CDPcholine	-	?

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Release 2023.1 (January 2023)