EC number:2.7.7.39

Enzyme

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     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.7 Nucleotidyltransferases
ID:2.7.7.39
Description:Glycerol-3-phosphate cytidylyltransferase.
Alternative Name: CDP-glycerol pyrophosphorylase.
CDP-glycerol diphosphorylase.
Cath: 3.40.50.620;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.7.39
BRENDA Enzyme Link: BRENDA 2.7.7.39
KEGG Enzyme Link: KEGG2.7.7.39
BioCyc Enzyme Link: BioCyc 2.7.7.39
ExPASy Enzyme Link: ExPASy2.7.7.39
EC2PDB Enzyme Link: EC2PDB 2.7.7.39
ExplorEnz Enzyme Link: ExplorEnz 2.7.7.39
PRIAM enzyme-specific profiles Link: PRIAM 2.7.7.39
IntEnz Enzyme Link: IntEnz 2.7.7.39
MEDLINE Enzyme Link: MEDLINE 2.7.7.39

EC number:2.7.7.39

MSA:

2.7.7.39;
Phylogenetic Tree:

2.7.7.39;
Uniprot:
M-CSA:
RHEA:13361 CTP + H(+) + sn-glycerol 3-phosphate = CDP-glycerol + diphosphate
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[P;H0;+0:4](=[*:5])(-[*:6])-[O;H0;+0:7]-[*:8].[H+;H0:9]>>[*:8]-[OH;+0:7].[*:3]-[P;H0;+0:4](=[*:5])(-[*:6])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Expression, purification, and characterization of CTP:glycerol-3-phosphate cytidylyltransferase from Bacillus subtilis.Park YS, Sweitzer TD, Dixon JE, Kent C1993 Aug 58393871
Glycerol-3-phosphate cytidylyltransferase. Structural changes induced by binding of CDP-glycerol and the role of lysine residues in catalysis.Pattridge KA, Weber CH, Friesen JA, Sanker S, Kent C, Ludwig ML2003 Dec 1914506262
CTP:glycerol 3-phosphate cytidylyltransferase (TarD) from Staphylococcus aureus catalyzes the cytidylyl transfer via an ordered Bi-Bi reaction mechanism with micromolar K(m) values.Badurina DS, Zolli-Juran M, Brown ED2003 Mar 2112637027
Negative cooperativity of substrate binding but not enzyme activity in wild-type and mutant forms of CTP:glycerol-3-phosphate cytidylyltransferase.Sanker S, Campbell HA, Kent C2001 Oct 1211487587