Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB03347"

Predicate	Value (sorted: default)
rdfs:label	"Triethyl Phosphate"
rdf:type	drugbank:drugs
drugbank:description	" experimental Karl-Heinz Mitschke, "Preparation of triethyl phosphate." U.S. Patent US20030100788, issued May 29, 2003. This compound belongs to the organophosphate esters. These are organic compounds containing phosphoric acid ester functional group. Organophosphate Esters Organic Compounds Organophosphorus Compounds Organic Phosphoric Acids and Derivatives Organophosphate Esters Organic Phosphoric Acids Polyamines polyamine logP 0.71 ALOGPS logS -1.1 ALOGPS Water Solubility 1.59e+01 g/l ALOGPS logP 1.18 ChemAxon IUPAC Name triethyl phosphate ChemAxon Traditional IUPAC Name triethyl phosphate ChemAxon Molecular Weight 182.1547 ChemAxon Monoisotopic Weight 182.07079548 ChemAxon SMILES CCOP(=O)(OCC)OCC ChemAxon Molecular Formula C6H15O4P ChemAxon InChI InChI=1S/C6H15O4P/c1-4-8-11(7,9-5-2)10-6-3/h4-6H2,1-3H3 ChemAxon InChIKey InChIKey=DQWPFSLDHJDLRL-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 44.76 ChemAxon Refractivity 42.34 ChemAxon Polarizability 17.86 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 1 ChemAxon H Bond Donor Count 0 ChemAxon pKa (strongest basic) -9.1 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon ChEBI 45927 PubChem Compound 6535 PubChem Substance 46508829 ChemSpider 6287 PDB TEN BE0001535 Parathion hydrolase Flavobacterium sp. (strain ATCC 27551) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Parathion hydrolase Involved in zinc ion binding Has an unusual substrate specificity for synthetic organophosphate triesters and phosphorofluoridates. All of the phosphate triesters found to be substrates are synthetic compounds. The identity of any naturally occurring substrate for the enzyme is unknown. Has no detectable activity with phosphate monoesters or diesters and no activity as an esterase or protease. It catalyzes the hydrolysis of the insecticide paraoxon at a rate approaching the diffusion limit and thus appears to be optimally evolved for utilizing this synthetic substrate opd Cell membrane; peripheral membrane protein None 8.48 39004.0 Flavobacterium sp. (strain ATCC 27551) GenBank Gene Database M29593 GenBank Protein Database 148713 UniProtKB P0A433 UniProt Accession OPD_FLAS2 EC 3.1.8.1 Parathion hydrolase precursor Phosphotriesterase PTE >Parathion hydrolase precursor MQTRRVVLKSAAAAGTLLGGLAGCASVAGSIGTGDRINTVRGPITISEAGFTLTHEHICG SSAGFLRAWPEFFGSRKALAEKAVRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAA DVHIVAATGLWFDPPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQ ELVLKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDTDDLSYL TALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTRALLIKALIDQGYMKQILVSN DWLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVIPFLREKGVPQETLAGITVTNPARFLSP TLRAS >1098 bp ATGCAAACGAGAAGGGTTGTGCTCAAGTCTGCGGCCGCCGCAGGAACTCTGCTCGGCGGC CTGGCTGGGTGCGCGAGCGTGGCTGGATCGATCGGCACAGGCGATCGGATCAATACCGTG CGCGGTCCTATCACAATCTCTGAAGCGGGTTTCACACTGACTCACGAGCACATCTGCGGC AGCTCGGCAGGATTCTTGCGTGCTTGGCCAGAGTTCTTCGGTAGCCGCAAAGCTCTAGCG GAAAAGGCTGTGAGAGGATTGCGCCGCGCCAGAGCGGCTGGCGTGCGAACGATTGTCGAT GTGTCGACTTTCGATATCGGTCGCGACGTCAGTTTATTGGCCGAGGTTTCGCGGGCTGCC GACGTTCATATCGTGGCGGCGACCGGCTTGTGGTTCGACCCGCCACTTTCGATGCGATTG AGGAGTGTAGAGGAACTCACACAGTTCTTCCTGCGTGAGATTCAATATGGCATCGAAGAC ACCGGAATTAGGGCGGGCATTATCAAGGTCGCGACCACAGGCAAGGCGACCCCCTTTCAG GAGTTAGTGTTAAAGGCGGCCGCCCGGGCCAGCTTGGCCACCGGTGTTCCGGTAACCACT CACACGGCAGCAAGTCAGCGCGATGGTGAGCAGCAGGCCGCCATTTTTGAGTCCGAAGGC TTGAGCCCCTCACGGGTTTGTATTGGTCACAGCGATGATACTGACGATTTGAGCTATCTC ACCGCCCTCGCTGCGCGCGGATACCTCATCGGTCTAGACCACATCCCGCACAGTGCGATT GGTCTAGAAGATAATGCGAGTGCATCAGCCCTCCTGGGCATCCGTTCGTGGCAAACACGG GCTCTCTTGATCAAGGCGCTCATCGACCAAGGCTACATGAAACAAATCCTCGTTTCGAAT GACTGGCTGTTCGGGTTTTCGAGCTATGTCACCAACATCATGGACGTGATGGATCGCGTG AACCCCGACGGGATGGCCTTCATTCCACTGAGAGTGATCCCATTCCTACGAGAGAAGGGC GTCCCACAGGAAACGCTGGCAGGCATCACTGTGACTAACCCGGCGCGGTTCTTGTCACCG ACCTTGCGGGCGTCATGA PF02126 PTE function ion binding function cation binding function transition metal ion binding function zinc ion binding function hydrolase activity, acting on ester bonds function binding function catalytic activity function hydrolase activity process catabolism process physiological process process metabolism BE0004036 Parathion hydrolase Brevundimonas diminuta # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Parathion hydrolase Involved in aryldialkylphosphatase activity Has an unusual substrate specificity for synthetic organophosphate triesters and phosphorofluoridates. All of the phosphate triesters found to be substrates are synthetic compounds. The identity of any naturally occurring substrate for the enzyme is unknown. Has no detectable activity with phosphate monoesters or diesters and no activity as an esterase or protease. It catalyzes the hydrolysis of the insecticide paraoxon at a rate approaching the diffusion limit and thus appears to be optimally evolved for utilizing this synthetic substrate opd Cell membrane None 8.48 39003.2 Brevundimonas diminuta GeneCards opd GenBank Gene Database M20392 GenBank Protein Database 151518 UniProtKB P0A434 UniProt Accession OPD_BREDI Phosphotriesterase PTE >Parathion hydrolase MQTRRVVLKSAAAAGTLLGGLAGCASVAGSIGTGDRINTVRGPITISEAGFTLTHEHICG SSAGFLRAWPEFFGSRKALAEKAVRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAA DVHIVAATGLWFDPPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQ ELVLKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDTDDLSYL TALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTRALLIKALIDQGYMKQILVSN DWLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVIPFLREKGVPQETLAGITVTNPARFLSP TLRAS >978 bp GTAAGCAATCGCAAGGGGGCAGCATGCAAACGAGAAGGGTTGTGCTCAAGTCTGCGGCCG CGAGAACTCTGCTCGGCGGCCTGGCTGGGTGCGCGACGTGGCTGGATCGATCGGCACAGG CGATGCGATCAATACGTGCGCGTCCTATCACAATCTCTGAAGCGGGTTTCACACTGACTC ACGAGGACATCTCGGCAGCTCGGCAGGATTCTTGCGTGCTTGGCCAGAGTTCTTCGGTAG CGCAAAGCTCTAGCGGAAAAGGCTGTGAGAGGATTGCGCGCCAGAGCGGCTGGCGTGCGA ACGATTGTCGATGTGTCGACTTTCGATATCGGTCGCGACGTCAGTTTATTGGCCGAGGTT TCGCGGGCTGCCGACGTTCATATCTGGCGGCGACCGGCTTGTGGTTCGACCCGCCACTTT CGATGCGATTGAGGTATGTAGAGGAACTCACACTAGTTCTTCCTGCGGTGAGATTCAATA TGGCATCGAAGTACACCGGAATTAGGGCGGGCATTATCAAGGTCGCGACCACAGGCAAGG CGACCCCCTTTCAGGAGTTAGTGTTAAAGGCGGCCGCCCGGGCCAGCTTGGCCACCGGTG TTCCGGTAACCACTCACACGGCAGCAAGTCAGCGCGATGGTGAGCGAGGCAGGCCGCCAT TTTTGAGTCCGAAGCTTGAGCCCTCACGGGTTTGTATTGGTCACAGCGATGATACTGACG ATTTGAGCTATCTCACCGCCCTGCTGCGCGGATACCTCATCGGTCTAGACCACATCCCGC ACAGTGCGATTGGTCTAGAAGATAATGCGAGTGCATCACCGCTCCTGGGCATCCGTTCGT GGCAAACACGGGCTCTCTTGATCAAGGCGCTCATCGACCAAGGCTACATGAAACAAATCC TCGTTTCGAATGACTGGCTGTTCGGGTTTTCGAGCTATGTCACCAACATCATGGACGTGA TGGATCGCGTGAACCCCG PF02126 PTE function cation binding function transition metal ion binding function zinc ion binding function hydrolase activity, acting on ester bonds function binding function catalytic activity function hydrolase activity function ion binding process catabolism process physiological process process metabolism "
owl:sameAs	drug:EXPT03038

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