Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB06890"

Predicate	Value (sorted: default)
rdfs:label	"(2R)-2-PHENYL-N-PYRIDIN-4-YLBUTANAMIDE"
rdf:type	drugbank:drugs
drugbank:description	" experimental This compound belongs to the phenylpropylamines. These are compounds containing a phenylpropylamine moiety, which consists of a phenyl group substituted at the third carbon by an propan-1-amine. Phenylpropylamines Organic Compounds Benzenoids Benzene and Substituted Derivatives Phenylpropylamines Aminopyridines and Derivatives Secondary Carboxylic Acid Amides Polyamines Carboxylic Acids Enolates aminopyridine pyridine secondary carboxylic acid amide carboxamide group polyamine enolate carboxylic acid derivative carboxylic acid amine organonitrogen compound logP 2.69 ALOGPS logS -3.1 ALOGPS Water Solubility 1.75e-01 g/l ALOGPS logP 2.82 ChemAxon IUPAC Name (2R)-2-phenyl-N-(pyridin-4-yl)butanamide ChemAxon Traditional IUPAC Name (2R)-2-phenyl-N-(pyridin-4-yl)butanamide ChemAxon Molecular Weight 240.3003 ChemAxon Monoisotopic Weight 240.126263144 ChemAxon SMILES [H][C@](CC)(C(=O)NC1=CC=NC=C1)C1=CC=CC=C1 ChemAxon Molecular Formula C15H16N2O ChemAxon InChI InChI=1S/C15H16N2O/c1-2-14(12-6-4-3-5-7-12)15(18)17-13-8-10-16-11-9-13/h3-11,14H,2H2,1H3,(H,16,17,18)/t14-/m1/s1 ChemAxon InChIKey InChIKey=MODBYAQUXXEFRM-CQSZACIVSA-N ChemAxon Polar Surface Area (PSA) 41.99 ChemAxon Refractivity 72.66 ChemAxon Polarizability 25.62 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 13.25 ChemAxon pKa (strongest basic) 5.65 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 670006 PubChem Substance 99443361 ChemSpider 583213 PDB 1CM BE0001730 Lanosterol 14-alpha demethylase Mycobacterium tuberculosis # 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 Lanosterol 14-alpha demethylase Secondary metabolites biosynthesis, transport and catabolism Its precise biological substrate is not known. Catalyzes C14-demethylation of lanosterol, 24,25-dihydrolanosterol and obtusifoliol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene- 3-beta-ol cyp51 Cytoplasm None 5.71 50878.0 Mycobacterium tuberculosis GenBank Gene Database BX842574 GenBank Protein Database 1550642 UniProtKB P0A512 UniProt Accession CP51_MYCTU CYPLI EC 1.14.13.70 Lanosterol 14-alpha demethylase P450-14DM P450-LIA1 Sterol 14- alpha demethylase >Cytochrome P450 51 MSAVALPRVSGGHDEHGHLEEFRTDPIGLMQRVRDECGDVGTFQLAGKQVVLLSGSHANE FFFRAGDDDLDQAKAYPFMTPIFGEGVVFDASPERRKEMLHNAALRGEQMKGHAATIEDQ VRRMIADWGEAGEIDLLDFFAELTIYTSSACLIGKKFRDQLDGRFAKLYHELERGTDPLA YVDPYLPIESFRRRDEARNGLVALVADIMNGRIANPPTDKSDRDMLDVLIAVKAETGTPR FSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHA LRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFP DPHDFVPARYEQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMA QPPESYRNDHSKMVVQLAQPACVRYRRRTGV >1356 bp TTAAACTCCCGTTCGCCGGCGGTAGCGCACGCAAGCGGGCTGGGCCAACTGCACCACCAT CTTCGAATGGTCGTTACGATAGCTTTCTGGCGGTTGCGCCATCTCAAACTCATACTCGCG CAACAACACCGAGAAGATCGCTTTGATCTGCATGATGGCGAACGCCGCCCCCACGCAACG ATGCCGGCCGGCGCCGAACGGAATCCACGTCCAGCGGTTGAGCAGATCTTCCTGGCGCGG CTGCTCGTATCGTGCTGGCACGAAGTCGTGGGGATCGGGGAAGTCTTCGGGGATCCGGTT GGAGATCGCCGGGGAGGCCGCCACCAGATCGCCCTCATGAATCCGGTGGCCTTGCACCTC GAACTCGCCCTTGGCCACTCGCATGAGGATGATCAGCGGAGGGTGCAGGCGCAGCGTCTC TTTCAGCACGTTTTCCAGCTGCGGAATCTGGCGCAGCGCATGGAAACTCACCGATCGGCC GTCGCCGTACAGCTCGTCGAGTTCGTCGATCACGGCCGCGTAGGCGTCGCGATGGCGCAT CAACTCGATCAGCGTCCACGAAGCCGTACCCGAGCTGGTGTGATGGCCGGCGAACATCAT CGAGATGAACATGCCGGTGATCTCGTCGGCCGAGAACCGGGGAGTGCCGGTCTCAGCCTT GACGGCGATGAGCACGTCGAGCATGTCACGGTCGCTCTTGTCGGTGGGTGGGTTGGCGAT CCGGCCGTTCATGATGTCCGCAACCAGTGCCACCAGACCATTGCGGGCTTCGTCGCGGCG ACGGAAGCTCTCGATCGGCAGATACGGGTCGACGTAGGCTAGTGGGTCGGTGCCGCGCTC CAACTCGTGATAGAGCTTGGCGAATCGCCCGTCGAGCTGGTCGCGGAACTTCTTGCCGAT CAGGCAGGCCGAGGAGGTGTAGATGGTCAGCTCGGCGAAGAAGTCCAGCAGATCGATCTC GCCGGCCTCACCCCAGTCGGCGATCATCCGTCGGACTTGATCTTCGATGGTGGCAGCGTG GCCCTTCATCTGCTCGCCGCGTAGCGCGGCATTGTGCAGCATCTCTTTACGCCGTTCCGG GCTGGCGTCGAACACCACGCCCTCGCCGAAGATCGGCGTCATGAACGGGTATGCCTTGGC CTGGTCCAGGTCGTCGTCGCCCGCCCGGAAGAAGAATTCGTTGGCGTGCGAGCCGGACAG CAGCACGACCTGCTTCCCGGCCAGCTGGAAGGTACCGACGTCTCCGCATTCGTCGCGGAC CCGTTGCATCAGCCCGATCGGATCGGTGCGGAACTCCTCGAGGTGGCCGTGTTCGTCGTG GCCACCCGAAACCCGGGGTAGTGCAACAGCGCTCAT PF00067 p450 function cation binding function transition metal ion binding function iron ion binding function binding function tetrapyrrole binding function catalytic activity function heme binding function monooxygenase activity function oxidoreductase activity function ion binding process generation of precursor metabolites and energy process electron transport process physiological process process metabolism process cellular metabolism "

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