Glycerophosphocholine cholinephosphodiesterase Structural studies References Navigation menu3.1.4.3860063-78-7 IntEnz viewBRENDA entryNiceZyme viewKEGG entrymetabolic pathwayprofileRCSB PDBPDBePDBsumAmiGO QuickGOarticlesarticlesproteins3.1.4.381WRA10.1016/0005-2760(75)90111-3166661eeexpanding ite
CholinesteraseAcetylcholinesteraseButyrylcholinesterasePectinesterase6-phosphogluconolactonasePAF acetylhydrolaseLipaseBile salt-dependentGastricLingualPancreaticLysosomalHormone-sensitiveEndothelialHepaticLipoproteinMonoacylglycerolDiacylglycerolPhospholipaseA1A2BCutinasePETaseAlkaline phosphataseALPIALPLALPPAcid phosphataseProstaticTartrate-resistant acid phosphatasePurple acid phosphatasesNucleotidaseGlucose 6-phosphataseFructose 1,6-bisphosphataseCalcineurinProtein phosphatasePP2AOCRLPyruvate dehydrogenase phosphataseFructose 6-P,2-kinase:fructose 2,6-bisphosphatasePTENPhytaseBeta-propeller phytaseInositol-phosphate phosphataseIMPA1IMPA2IMPA3Protein phosphataseProtein tyrosine phosphataseProtein serine/threonine phosphataseDual-specificity phosphatasearylsulfataseArylsulfatase AArylsulfatase BArylsulfatase ESteroid sulfataseGalactosamine-6 sulfataseIduronate-2-sulfataseN-acetylglucosamine-6-sulfataseRecBCDOligonucleotidaseDeoxyribonuclease IDeoxyribonuclease IIDeoxyribonuclease IVRestriction enzymeUvrABC endonucleaseRNase IIIRNase H12A2B2CRNase PRNase A1234/5RNase T1RNA-induced silencing complexAspergillus nuclease S1Micrococcal nucleaseActive siteBinding siteCatalytic triadOxyanion holeEnzyme promiscuityCatalytically perfect enzymeCoenzymeCofactorEnzyme catalysisEC numberEnzyme superfamilyEnzyme familyList of enzymesOxidoreductaseslistTransferaseslistHydrolaseslistLyaseslistIsomeraseslistLigaseslistTranslocaseslist
EC 3.1.4Enzymes of known structure
enzymologyEC3.1.4.38enzymecatalyzeschemical reactionsubstratessn-glycero-3-phosphocholineH2Oproductsglycerolcholine phosphatehydrolasesdiestersystematic namestructurePDB1WRA
| glycerophosphocholine cholinephosphodiesterase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.1.4.38 | ||||||||
| CAS number | 60063-78-7 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a glycerophosphocholine cholinephosphodiesterase (EC 3.1.4.38) is an enzyme that catalyzes the chemical reaction
- sn-glycero-3-phosphocholine + H2O ⇌displaystyle rightleftharpoons glycerol + choline phosphate
Thus, the two substrates of this enzyme are sn-glycero-3-phosphocholine and H2O, whereas its two products are glycerol and choline phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name of this enzyme class is sn-glycero-3-phosphocholine cholinephosphohydrolase. This enzyme is also called L-3-glycerylphosphinicocholine cholinephosphohydrolase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1WRA.
References
Abra RM, Quinn PJ (1975). "A novel pathway for phosphatidylcholine catabolism in rat brain homogenates". Biochim. Biophys. Acta. 380 (3): 436–41. doi:10.1016/0005-2760(75)90111-3. PMID 166661..mw-parser-output cite.citationfont-style:inherit.mw-parser-output .citation qquotes:"""""""'""'".mw-parser-output .citation .cs1-lock-free abackground:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center.mw-parser-output .citation .cs1-lock-limited a,.mw-parser-output .citation .cs1-lock-registration abackground:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center.mw-parser-output .citation .cs1-lock-subscription abackground:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registrationcolor:#555.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration spanborder-bottom:1px dotted;cursor:help.mw-parser-output .cs1-ws-icon abackground:url("//upload.wikimedia.org/wikipedia/commons/thumb/4/4c/Wikisource-logo.svg/12px-Wikisource-logo.svg.png")no-repeat;background-position:right .1em center.mw-parser-output code.cs1-codecolor:inherit;background:inherit;border:inherit;padding:inherit.mw-parser-output .cs1-hidden-errordisplay:none;font-size:100%.mw-parser-output .cs1-visible-errorfont-size:100%.mw-parser-output .cs1-maintdisplay:none;color:#33aa33;margin-left:0.3em.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-formatfont-size:95%.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-leftpadding-left:0.2em.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-rightpadding-right:0.2em
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