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Phosphatidate cytidylyltransferase

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phosphatidate cytidylyltransferase
Identifiers
EC no.2.7.7.41
CAS no.9067-83-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Protein family
Cytidylyltransferase family
Identifiers
SymbolCTP_transf_1
PfamPF01148
InterProIPR000374
PROSITEPDOC01019
OPM superfamily414
OPM protein4q2e
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Phosphatidate cytidylyltransferase (EC 2.7.7.41) (also known as CDP- diacylglycerol synthase) (CDS) is the enzyme that catalyzes the synthesis of CDP-diacylglycerol from cytidine triphosphate and phosphatidate.

CTP + phosphatidate {\displaystyle \rightleftharpoons } diphosphate + CDP-diacylglycerol

Thus, the two substrates of this enzyme are cytidine triphosphate, or CTP, and phosphatidate, whereas its two products are diphosphate and CDP-diacylglycerol.

CDP-diacylglycerol is an important branch point intermediate in both prokaryotic and eukaryotic organisms. CDS is a membrane-bound enzyme.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is CTP:phosphatidate cytidylyltransferase. Other names in common use include CDP diglyceride pyrophosphorylase, CDP-diacylglycerol synthase, CDP-diacylglyceride synthetase, cytidine diphosphoglyceride pyrophosphorylase, phosphatidate cytidyltransferase, phosphatidic acid cytidylyltransferase, CTP:1,2-diacylglycerophosphate-cytidyl transferase, CTP-diacylglycerol synthetase, DAG synthetase, and CDP-DG. This enzyme participates in glycerophospholipid metabolism and phosphatidylinositol signaling system.

References

  1. Sparrow CP, Raetz CR (1985). "Purification and properties of the membrane-bound CDP-diglyceride synthetase from Escherichia coli". Journal of Biological Chemistry. 260 (22): 12084–12091. doi:10.1016/S0021-9258(17)38989-5. PMID 2995359.
  2. Shen H, Heacock PN, Clancey CJ, Dowhan W (1996). "The CDS1 gene encoding CDP-diacylglycerol synthase in Saccharomyces cerevisiae is essential for cell growth". Journal of Biological Chemistry. 271 (2): 789–795. doi:10.1074/jbc.271.2.789. PMID 8557688.
  3. Kondo H, Goto K, Saito S, Tonosaki A (1997). "Gene cloning and characterization of CDP-diacylglycerol synthase from rat brain". Journal of Biological Chemistry. 272 (14): 9503–9509. doi:10.1074/jbc.272.14.9503. PMID 9083091.
Transferases: phosphorus-containing groups (EC 2.7)
2.7.1-2.7.4:
phosphotransferase/kinase
(PO4)
2.7.1: OH acceptor
2.7.2: COOH acceptor
2.7.3: N acceptor
2.7.4: PO4 acceptor
2.7.6: diphosphotransferase
(P2O7)
2.7.7: nucleotidyltransferase
(PO4-nucleoside)
Polymerase
DNA polymerase
DNA-directed DNA polymerase
I/A
γ
θ
ν
T7
Taq
II/B
α
δ
ε
ζ
Pfu
III/C
IV/X
β
λ
μ
TDT
V/Y
η
ι
κ
RNA-directed DNA polymerase
Reverse transcriptase
Telomerase
RNA polymerase
Template-directed
RNA polymerase I
II
III
IV
V
ssRNAP
POLRMT
Primase
1
2
PrimPol
RNA-dependent RNA polymerase
Polyadenylation
PAP
PNPase
Phosphorolytic
3' to 5' exoribonuclease
Nucleotidyltransferase
Guanylyltransferase
Other
2.7.8: miscellaneous
Phosphatidyltransferases
Glycosyl-1-phosphotransferase
2.7.10-2.7.13: protein kinase
(PO4; protein acceptor)
2.7.10: protein-tyrosine
2.7.11: protein-serine/threonine
2.7.12: protein-dual-specificity
2.7.13: protein-histidine
Enzymes
Activity
Regulation
Classification
Kinetics
Types
Portal:


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