Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB08523"

Predicate	Value (sorted: none)
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 Polyamines polyamine amine organonitrogen compound logP 0.88 ALOGPS logS -1.2 ALOGPS Water Solubility 1.15e+01 g/l ALOGPS logP 1.3 ChemAxon IUPAC Name [N-hydroxy-N-(3-phenylpropyl)amino]methanol ChemAxon Traditional IUPAC Name [N-hydroxy-N-(3-phenylpropyl)amino]methanol ChemAxon Molecular Weight 181.2316 ChemAxon Monoisotopic Weight 181.110278729 ChemAxon SMILES OCN(O)CCCC1=CC=CC=C1 ChemAxon Molecular Formula C10H15NO2 ChemAxon InChI InChI=1S/C10H15NO2/c12-9-11(13)8-4-7-10-5-2-1-3-6-10/h1-3,5-6,12-13H,4,7-9H2 ChemAxon InChIKey InChIKey=GELOPWXSYZDPJT-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 43.7 ChemAxon Refractivity 51.53 ChemAxon Polarizability 20.3 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 13.45 ChemAxon pKa (strongest basic) 0.19 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 5289329 PubChem Substance 99444994 ChemSpider 4451319 PDB SB7 BE0002536 Peptide deformylase Streptococcus pneumoniae (strain ATCC BAA-255 / R6) # 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 Peptide deformylase Involved in iron ion binding Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity) def Cytoplasmic None 4.87 22692.0 Streptococcus pneumoniae (strain ATCC BAA-255 / R6) GenBank Gene Database AE008502 UniProtKB Q8DP79 UniProt Accession DEF_STRR6 EC 3.5.1.88 PDF Polypeptide deformylase >Peptide deformylase MSAIERITKAAHLIDMNDIIREGNPTLRTVAEEVTFPLSDQEIILGEKMMQFLKHSQDPV MAEKMGLRGGVGLAAPQLDISKRIIAVLVPNIVEEGETPQEAYDLEAIMYNPKIVSHSVQ DAALGEGEGCLSVDRNVPGYVVRHARVTVDYFDKDGEKHRIKLKGYNSIVVQHEIDHING IMFYDRINEKDPFAVKDGLLILE >612 bp ATGTCTGCAATAGAACGTATTACAAAAGCTGCTCACTTAATTGATATGAACGATATTATC CGTGAAGGGAATCCTACTCTACGCACGGTTGCTGAGGAAGTCACTTTCCCCCTATCTGAC CAGGAAATCATCCTAGGCGAAAAGATGATGCAATTCCTTAAACATTCCCAAGATCCTGTC ATGGCTGAAAAAATGGGACTCCGCGGTGGTGTTGGACTGGCTGCTCCCCAGTTAGATATC TCAAAACGCATTATCGCTGTTTTGGTACCTAATATTGTTGAAGAAGGCGAAACTCCACAG GAAGCCTACGATTTGGAAGCCATTATGTACAATCCAAAAATCGTCTCTCACTCTGTTCAA GATGCTGCTCTTGGCGAAGGAGAAGGTTGCCTGTCTGTTGACCGTAACGTGCCTGGCTAT GTTGTTCGCCATGCCCGCGTTACTGTTGACTACTTTGACAAAGATGGAGAAAAACACCGT ATCAAACTCAAAGGCTACAACTCCATTGTTGTTCAGCATGAAATTGACCACATTAACGGT ATCATGTTTTACGATCGCATCAATGAAAAAGACCCATTTGCAGTTAAAGATGGTTTACTG ATTCTTGAATAA PF01327 Pep_deformylase function peptide deformylase activity function hydrolase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides function ion binding function cation binding function transition metal ion binding function binding function iron ion binding function catalytic activity process metabolism process macromolecule metabolism process physiological process process macromolecule biosynthesis process protein biosynthesis BE0001475 Peptide deformylase Escherichia coli (strain K12) # 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 Peptide deformylase Translation, ribosomal structure and biogenesis Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions def Cytoplasmic None 5.0 19329.0 Escherichia coli (strain K12) GenBank Gene Database X77800 GenBank Protein Database 471304 UniProtKB P0A6K3 UniProt Accession DEF_ECOLI EC 3.5.1.88 PDF Polypeptide deformylase >Peptide deformylase MSVLQVLHIPDERLRKVAKPVEEVNAEIQRIVDDMFETMYAEEGIGLAATQVDIHQRIIV IDVSENRDERLVLINPELLEKSGETGIEEGCLSIPEQRALVPRAEKVKIRALDRDGKPFE LEADGLLAICIQHEMDHLVGKLFMDYLSPLKQQRIRQKVEKLDRLKARA >510 bp ATGTCAGTTTTGCAAGTGTTACATATTCCGGACGAGCGGCTTCGCAAAGTTGCTAAACCG GTAGAAGAAGTGAATGCAGAAATTCAGCGTATCGTCGATGATATGTTCGAGACGATGTAC GCAGAAGAAGGTATTGGCCTGGCGGCAACCCAGGTTGATATCCATCAACGTATCATTGTT ATTGATGTTTCGGAAAACCGTGACGAACGGCTAGTGTTAATCAATCCAGAGCTTTTAGAA AAAAGCGGCGAAACAGGCATTGAAGAAGGTTGCCTGTCGATCCCTGAACAACGTGCTTTA GTGCCGCGCGCAGAGAAAGTTAAAATTCGCGCCCTTGACCGCGACGGTAAACCATTTGAA CTGGAAGCAGACGGTCTGTTAGCCATCTGTATTCAGCATGAGATGGATCACCTGGTCGGC AAACTGTTTATGGATTATCTGTCACCGCTGAAACAACAACGTATTCGTCAGAAAGTTGAA AAACTGGATCGTCTGAAAGCCCGGGCTTAA PF01327 Pep_deformylase function ion binding function cation binding function transition metal ion binding function binding function iron ion binding function catalytic activity function peptide deformylase activity function hydrolase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides process physiological process process macromolecule biosynthesis process protein biosynthesis process metabolism process macromolecule metabolism "
rdfs:label	"[HYDROXY(3-PHENYLPROPYL)AMINO]METHANOL"

All properties reside in the graph file:///home/swish/src/ClioPatria/guidelines3/drugbank_small.nt

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