Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB07736"

Predicate	Value (sorted: default)
rdfs:label	"(2S)-4-(4-fluorobenzyl)-N-(2-sulfanylethyl)piperazine-2-carboxamide"
rdf:type	drugbank:drugs
drugbank:description	" experimental This compound belongs to the piperazine carboxamides. These are heterocyclic compounds containing a piperazine ring substituted by one or more carboxamide group. Piperazine Carboxamides Organic Compounds Heterocyclic Compounds Piperazines Piperazine Carboxylic Acids and Derivatives Fluorobenzenes Aryl Fluorides Diazinanes Secondary Carboxylic Acid Amides Tertiary Amines Enolates Alkylthiols Dialkylamines Polyamines Carboxylic Acids Organofluorides fluorobenzene aryl halide aryl fluoride 1,4-diazinane benzene secondary carboxylic acid amide carboxamide group tertiary amine polyamine secondary amine alkylthiol enolate carboxylic acid derivative secondary aliphatic amine carboxylic acid organohalogen organofluoride organonitrogen compound amine logP 1.17 ALOGPS logS -3.6 ALOGPS Water Solubility 7.12e-02 g/l ALOGPS logP 1.03 ChemAxon IUPAC Name (2S)-4-[(4-fluorophenyl)methyl]-N-(2-sulfanylethyl)piperazine-2-carboxamide ChemAxon Traditional IUPAC Name (2S)-4-[(4-fluorophenyl)methyl]-N-(2-sulfanylethyl)piperazine-2-carboxamide ChemAxon Molecular Weight 297.392 ChemAxon Monoisotopic Weight 297.131111172 ChemAxon SMILES [H][C@]1(CN(CC2=CC=C(F)C=C2)CCN1)C(=O)NCCS ChemAxon Molecular Formula C14H20FN3OS ChemAxon InChI InChI=1S/C14H20FN3OS/c15-12-3-1-11(2-4-12)9-18-7-5-16-13(10-18)14(19)17-6-8-20/h1-4,13,16,20H,5-10H2,(H,17,19)/t13-/m0/s1 ChemAxon InChIKey InChIKey=CEXXKSSFAKABEN-ZDUSSCGKSA-N ChemAxon Polar Surface Area (PSA) 44.37 ChemAxon Refractivity 80.6 ChemAxon Polarizability 31.29 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 10.08 ChemAxon pKa (strongest basic) 8.06 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 25134251 PubChem Substance 99444207 PDB F1J BE0000988 Beta-secretase 1 Human # 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 Beta-secretase 1 Involved in aspartic-type signal peptidase activity Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase BACE1 11q23.2-q23.3 Membrane; single-pass type I membrane protein 458-478 5.19 55764.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:933 GenAtlas BACE1 GeneCards BACE1 GenBank Gene Database AF190725 GenBank Protein Database 6118539 UniProtKB P56817 UniProt Accession BACE1_HUMAN Asp 2 ASP2 Aspartyl protease 2 Beta-secretase 1 precursor Beta-site amyloid precursor protein cleaving enzyme 1 Beta-site APP cleaving enzyme 1 EC 3.4.23.46 Memapsin-2 Membrane-associated aspartic protease 2 >Beta-secretase 1 precursor MAQALPWLLLWMGAGVLPAHGTQHGIRLPLRSGLGGAPLGLRLPRETDEEPEEPGRRGSF VEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFLHRYYQRQLSST YRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEGIL GLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCGAGFPLNQSEVLASVGGSMIIGGI DHSLYTGSLWYTPIRREWYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKK VFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRIT ILPQQYLRPVEDVATSQDDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSAC HVHDEFRTAAVEGPFVTLDMEDCGYNIPQTDESTLMTIAYVMAAICALFMLPLCLMVCQW RCLRCLRQQHDDFADDISLLK >1506 bp ATGGCCCAAGCCCTGCCCTGGCTCCTGCTGTGGATGGGCGCGGGAGTGCTGCCTGCCCAC GGCACCCAGCACGGCATCCGGCTGCCCCTGCGCAGCGGCCTGGGGGGCGCCCCCCTGGGG CTGCGGCTGCCCCGGGAGACCGACGAAGAGCCCGAGGAGCCCGGCCGGAGGGGCAGCTTT GTGGAGATGGTGGACAACCTGAGGGGCAAGTCGGGGCAGGGCTACTACGTGGAGATGACC GTGGGCAGCCCCCCGCAGACGCTCAACATCCTGGTGGATACAGGCAGCAGTAACTTTGCA GTGGGTGCTGCCCCCCACCCCTTCCTGCATCGCTACTACCAGAGGCAGCTGTCCAGCACA TACCGGGACCTCCGGAAGGGTGTGTATGTGCCCTACACCCAGGGCAAGTGGGAAGGGGAG CTGGGCACCGACCTGGTAAGCATCCCCCATGGCCCCAACGTCACTGTGCGTGCCAACATT GCTGCCATCACTGAATCAGACAAGTTCTTCATCAACGGCTCCAACTGGGAAGGCATCCTG GGGCTGGCCTATGCTGAGATTGCCAGGCCTGACGACTCCCTGGAGCCTTTCTTTGACTCT CTGGTAAAGCAGACCCACGTTCCCAACCTCTTCTCCCTGCAGCTTTGTGGTGCTGGCTTC CCCCTCAACCAGTCTGAAGTGCTGGCCTCTGTCGGAGGGAGCATGATCATTGGAGGTATC GACCACTCGCTGTACACAGGCAGTCTCTGGTATACACCCATCCGGCGGGAGTGGTATTAT GAGGTGATCATTGTGCGGGTGGAGATCAATGGACAGGATCTGAAAATGGACTGCAAGGAG TACAACTATGACAAGAGCATTGTGGACAGTGGCACCACCAACCTTCGTTTGCCCAAGAAA GTGTTTGAAGCTGCAGTCAAATCCATCAAGGCAGCCTCCTCCACGGAGAAGTTCCCTGAT GGTTTCTGGCTAGGAGAGCAGCTGGTGTGCTGGCAAGCAGGCACCACCCCTTGGAACATT TTCCCAGTCATCTCACTCTACCTAATGGGTGAGGTTACCAACCAGTCCTTCCGCATCACC ATCCTTCCGCAGCAATACCTGCGGCCAGTGGAAGATGTGGCCACGTCCCAAGACGACTGT TACAAGTTTGCCATCTCACAGTCATCCACGGGCACTGTTATGGGAGCTGTTATCATGGAG GGCTTCTACGTTGTCTTTGATCGGGCCCGAAAACGAATTGGCTTTGCTGTCAGCGCTTGC CATGTGCACGATGAGTTCAGGACGGCAGCGGTGGAAGGCCCTTTTGTCACCTTGGACATG GAAGACTGTGGCTACAACATTCCACAGACAGATGAGTCAACCCTCATGACCATAGCCTAT GTCATGGCTGCCATCTGCGCCCTCTTCATGCTGCCACTCTGCCTCATGGTGTGTCAGTGG CGCTGCCTCCGCTGCCTGCGCCAGCAGCATGATGACTTTGCTGATGACATCTCCCTGCTG AAGTGA PF00026 Asp function hydrolase activity function peptidase activity function endopeptidase activity function pepsin A activity function aspartic-type endopeptidase activity function catalytic activity function aspartic-type signal peptidase activity process metabolism process macromolecule metabolism process protein metabolism process cellular protein metabolism process proteolysis process physiological process "

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