Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB07907"

Predicate	Value (sorted: none)
rdfs:label	"(2S)-2-HYDROXYOCTANOIC ACID"
rdf:type	ns1:drugs
ns1:description	" experimental This compound belongs to the medium-chain hydroxy acids and derivatives. These are hydroxy acids with a 6 to 12 carbon atoms long side chain. Medium-chain Hydroxy Acids and Derivatives Organic Compounds Organic Acids and Derivatives Hydroxy Acids and Derivatives Medium-chain Hydroxy Acids and Derivatives Fatty Alcohols Alpha Hydroxy Acids and Derivatives Fatty Acids and Conjugates Secondary Alcohols Enolates Polyamines Carboxylic Acids Aldehydes alpha-hydroxy acid secondary alcohol polyamine enolate carboxylic acid carboxylic acid derivative alcohol aldehyde logP 1.8 ALOGPS logS -1.2 ALOGPS Water Solubility 1.12e+01 g/l ALOGPS logP 1.83 ChemAxon IUPAC Name (2S)-2-hydroxyoctanoic acid ChemAxon Traditional IUPAC Name (2S)-2-hydroxyoctanoic acid ChemAxon Molecular Weight 160.2108 ChemAxon Monoisotopic Weight 160.109944378 ChemAxon SMILES [H][C@](O)(CCCCCC)C(O)=O ChemAxon Molecular Formula C8H16O3 ChemAxon InChI InChI=1S/C8H16O3/c1-2-3-4-5-6-7(9)8(10)11/h7,9H,2-6H2,1H3,(H,10,11)/t7-/m0/s1 ChemAxon InChIKey InChIKey=JKRDADVRIYVCCY-ZETCQYMHSA-N ChemAxon Polar Surface Area (PSA) 57.53 ChemAxon Refractivity 41.77 ChemAxon Polarizability 18.19 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 4.42 ChemAxon pKa (strongest basic) -3.8 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 6995013 PubChem Substance 99444378 ChemSpider 5362983 PDB HOC BE0003766 Hydroxyacid oxidase 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 Hydroxyacid oxidase 1 Energy production and conversion Has 2-hydroxyacid oxidase activity. Most active on the 2-carbon substrate glycolate, but is also active on 2-hydroxy fatty acids HAO1 20p12 Peroxisome None 8.29 40923.9 Human HUGO Gene Nomenclature Committee (HGNC) GNC:4809 GeneCards HAO1 GenBank Gene Database AF244134 GenBank Protein Database 7530485 UniProtKB Q9UJM8 UniProt Accession HAOX1_HUMAN Glycolate oxidase GOX HAOX1 >Hydroxyacid oxidase 1 MLPRLICINDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAET DLSTSVLGQRVSMPICVGATAMQRMAHVDGELATVRACQSLGTGMMLSSWATSSIEEVAE AGPEALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYLGNRLDDVRNRFKLPPQ LRMKNFETSTLSFSPEENFGDDSGLAAYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILR GDDAREAVKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDV LKALALGAKAVFVGRPIVWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLV RKNPLAVSKI PF01070 FMN_dh function catalytic activity function nucleotide binding function FMN binding function oxidoreductase activity function binding process metabolism process cellular metabolism process generation of precursor metabolites and energy process electron transport process physiological process BE0003028 (S)-mandelate dehydrogenase Pseudomonas putida # 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 (S)-mandelate dehydrogenase Involved in catalytic activity Reduction of L(+)-mandelate to benzoylformate mdlB None 8.22 43438.0 Pseudomonas putida GenBank Gene Database AY143338 UniProtKB P20932 UniProt Accession MDLB_PSEPU EC 1.-.-.- MDH S-mandelate dehydrogenase >L(+)-mandelate dehydrogenase MSQNLFNVEDYRKLRQKRLPKMVYDYLEGGAEDEYGVKHNRDVFQQWRFKPKRLVDVSRR SLQAEVLGKRQSMPLLIGPTGLNGALWPKGDLALARAATKAGIPFVLSTASNMSIEDLAR QCDGDLWFQLYVIHREIAQGMVLKALHTGYTTLVLTTDVAVNGYRERDLHNRFKIPMSYS AKVVLDGCLHPRWSLDFVRHGMPQLANFVSSQTSSLEMQAALMSRQMDASFNWEALRWLR DLWPHKLLVKGLLSAEDADRCIAEGADGVILSNHGGRQLDCAISPMEVLAQSVAKTGKPV LIDSGFRRGSDIVKALALGAEAVLLGRATLYGLAARGETGVDEVLTLLKADIDRTLAQIG CPDITSLSPDYLQNEGVTNTAPVDHLIGKGTHA >1182 bp TCATGCGTGTGTTCCTTTACCAATGAGGTGATCGACTGGAGCGGTGTTAGTCACTCCCTC GTTTTGGAGGTAATCAGGAGAAAGGGAGGTGATGTCAGGGCATCCAATCTGGGCAAGGGT GCGGTCGATATCCGCTTTTAGGAGGGTTAGCACCTCGTCAACACCCGTTTCACCTCGTGC TGCAAGGCCATACAAAGTTGCACGACCCAGGAGTACAGCCTCAGCACCTAGCGCAAGTGC TTTAACGATGTCCGAACCCCGTCGGAAGCCGCTATCGATAAGCACTGGTTTTCCAGTTTT CGCTACCGATTGAGCCAAAACTTCCATTGGCGATATCGCGCAATCGAGTTGGCGACCGCC GTGGTTTGATAGGATTACGCCGTCTGCACCTTCAGCGATGCACCGATCGGCGTCCTCAGC ACTGAGCAACCCCTTTACGAGGAGTTTGTGCGGCCAGAGGTCACGCAGCCATCTCAATGC CTCCCAGTTGAAACTGGCATCCATTTGGCGGCTCATCAATGCTGCCTGCATTTCTAAGCT AGACGTTTGACTGCTGACGAAATTGGCCAGTTGCGGCATGCCGTGTCGCACGAAGTCGAG CGACCAGCGCGGATGCAGGCATCCGTCCAGCACCACCTTTGCGGAGTAGCTCATTGGTAT CTTGAATCGGTTATGCAGGTCGCGCTCGCGATAGCCGTTAACCGCCACATCCGTAGTAAG CACCAGTGTCGTGTAACCAGTGTGCAGGGCTTTGAGCACCATCCCCTGCGCAATCTCTCG GTGGATCACATAGAGCTGGAACCACAGATCGCCATCACACTGACGTGCGAGGTCTTCAAT GGACATGTTGGAGGCGGTCGACAGCACGAACGGGATTCCGGCCTTGGTTGCTGCTCGAGC TAAAGCGAGATCCCCCTTAGGCCACAGCGCACCGTTCAGCCCAGTAGGCCCAATCAAGAG AGGCATCGACTGCCTCTTTCCAAGTACTTCCGCTTGGAGGCTGCGGCGGCTGACGTCTAC TAGCCGCTTCGGTTTGAATCGCCATTGCTGGAAGACGTCGCGGTTGTGTTTCACCCCGTA TTCGTCTTCAGCCCCACCTTCCAGATAGTCGTAGACCATCTTCGGCAAGCGCTTTTGCCG AAGCTTGCGATAGTCCTCAACGTTAAAGAGATTCTGGCTCAT PF01070 FMN_dh function binding function catalytic activity function nucleotide binding function FMN binding function oxidoreductase activity process generation of precursor metabolites and energy process electron transport process physiological process process metabolism process cellular metabolism "

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

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