BRENDA - Enzyme Database

A prototypical cytidylyltransferase: CTP:glycerol-3-phosphate cytidylyltransferase from Bacillus subtilis

Weber, C.H.; Park, Y.S.; Sanker, S.; Kent, C.; Ludwig, M.L.; Structure Fold. Des. 7, 1113-1124 (1999)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
2.7.7.41
hanging-drop method
Bacillus subtilis
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
2.7.7.41
Bacillus subtilis
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.7.7.41
CTP + phosphatidate
-
643317
Bacillus subtilis
diphosphate + CDPdiacylglycerol
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
2.7.7.41
More
as determined from crystal structure the enzyme is a homodimer, each monomer comprises an alpha/beta fold with a central 3-2-1-4-5 parallel beta sheet
Bacillus subtilis
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
2.7.7.41
hanging-drop method
Bacillus subtilis
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.7.7.41
CTP + phosphatidate
-
643317
Bacillus subtilis
diphosphate + CDPdiacylglycerol
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
2.7.7.41
More
as determined from crystal structure the enzyme is a homodimer, each monomer comprises an alpha/beta fold with a central 3-2-1-4-5 parallel beta sheet
Bacillus subtilis