Phosphatidate cytidylyltransferase
phosphatidate cytidylyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.7.7.41 | ||||||||
CAS no. | 9067-83-8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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Cytidylyltransferase family | |||||||||
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Identifiers | |||||||||
Symbol | CTP_transf_1 | ||||||||
Pfam | PF01148 | ||||||||
InterPro | IPR000374 | ||||||||
PROSITE | PDOC01019 | ||||||||
OPM superfamily | 414 | ||||||||
OPM protein | 4q2e | ||||||||
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Phosphatidate cytidylyltransferase (EC 2.7.7.41)[1][2][3] (also known as CDP- diacylglycerol synthase) (CDS) is the enzyme that catalyzes the synthesis of CDP-diacylglycerol from cytidine triphosphate and phosphatidate.
- CTP + phosphatidate 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
[edit]- ^ 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.
- ^ 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.
- ^ 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.
- Carter JR, Kennedy EP (1966). "Enzymatic synthesis of cytidine diphosphate diglyceride". Journal of Lipid Research. 7 (5): 678–83. doi:10.1016/S0022-2275(20)39250-6. PMID 4291255.
- McCaman RE, Finnerty WR (1968). "Biosynthesis of cytidine diphosphate-diglyceride by a particulate fracgion from Micrococcus cerificans". Journal of Biological Chemistry. 243 (19): 5074–80. doi:10.1016/S0021-9258(18)91993-9. PMID 5679981.
- Petzold GL, Agranoff BW (1967). "The biosynthesis of cytidine diphosphate diglyceride by embryonic chick brain". Journal of Biological Chemistry. 242 (6): 1187–91. doi:10.1016/S0021-9258(18)96162-4. PMID 6067194.