http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CA-2330733-A1
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_58498ab5182117cfa1bba22e33f64947 http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_e6f0c8331c288c3f5779bc1a3ff0f937 |
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A23L33-12 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P13-001 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P7-6463 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P7-6481 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Q1-6883 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-1288 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A23L1-30 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-12 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12Q1-6883 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12Q1-68 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-54 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P7-64 |
| filingDate | 1999-06-07-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_bb8753feedf6e778d5cd1c8cd78af91f http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_88a12ee1085453ad702041ae4902409d |
| publicationDate | 1999-12-16-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | CA-2330733-A1 |
| titleOfInvention | Cloning of human choline/ethanolaminephosphotransferases; synthesis of phosphatidylcholine, phosphatidylethanolamine, and platelet activating factor |
| abstract | We report the first cloning and expression, from a mammalian source, of proteins capable of catalyzing choline- and ethanolaminephosphotransferase reactions (hCEPT1 and hCEPT2). Both coding regions predict highly hydrophobic proteins of 43-46.5 kDa with several predicted membrane spanning domains. A CDP-alcohol phosphotransferase motif, DG(x)2AR(x)8G(x)3D(x)3D, has been identified in both hCEPT1 and hCEPT2 choline- and ethanolamine-phosphotransferases (and several other lipid synthesizing enzymes that catalyze the formation of a phosphoester bond by the displacement of CMP from a CDP-alcohol by a second alcohol). Site-directed mutagenesis was used to differentiate the residues responsible for choline- versus ethanolamine-phosphotransferase activity. Mutation of glycine 156 of hCEPT1 abolished ethanolaminephosphotransferase activity, while cholinephosphotransferase activity remained intact. |
| priorityDate | 1998-06-08-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 111.