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Literature summary for 2.7.7.39 extracted from

  • Sanker, S.; Campbell, H.A.; Kent, C.
    Negative cooperativity of substrate binding but not enzyme activity in wild-type and mutant forms of CTP:glycerol-3-phosphate cytidylyltransferase (2001), J. Biol. Chem., 276, 37922-37928.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
D94A initial binding constant is similar to wild-type enzyme Bacillus subtilis
D94A/H14A binding constants for CTP and glycerol 3-phosphate are similar to wild-type enzyme Bacillus subtilis
H14A Kd value for binding of a single substrate is similar to those for the wild-type enzyme Bacillus subtilis
H17A initial binding constant is similar to wild-type enzyme Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
CTP + sn-glycerol 3-phosphate Bacillus subtilis
-
diphosphate + CDPglycerol
-
?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Bacillus subtilis

Reaction

Reaction Comment Organism Reaction ID
CTP + sn-glycerol 3-phosphate = diphosphate + CDP-glycerol mechanism Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CTP + sn-glycerol 3-phosphate
-
Bacillus subtilis diphosphate + CDPglycerol
-
?