{"ymdb_id":"YMDB00842","created_at":"2011-05-29T18:57:31.000Z","updated_at":"2016-09-08T18:35:58.000Z","name":"24,25-dihydrolanosterol","cas":"79-62-9","state":"Solid","melting_point":null,"description":"24,25-Dihydrolanosterol is involved in the biosynthesis of steroids. 24,25-Dihydrolanosterol is reversibly converted to lanosterol by delta24-sterol reductase [EC:1.3.1.72].","experimental_water_solubility":null,"experimental_logp_hydrophobicity":null,"location":null,"synthesis_reference":null,"chebi_id":"28113","hmdb_id":"HMDB06839","kegg_id":"C05109","pubchem_id":"440560","cs_id":null,"foodb_id":null,"wikipedia_link":null,"biocyc_id":"CPD-8606","iupac":"(2S,5S,7R,11R,14R,15R)-2,6,6,11,15-pentamethyl-14-[(2R)-6-methylheptan-2-yl]tetracyclo[8.7.0.0^{2,7}.0^{11,15}]heptadec-1(10)-en-5-ol","traditional_iupac":"(2S,5S,7R,11R,14R,15R)-2,6,6,11,15-pentamethyl-14-[(2R)-6-methylheptan-2-yl]tetracyclo[8.7.0.0^{2,7}.0^{11,15}]heptadec-1(10)-en-5-ol","logp":"8.112252002333333","pka":null,"alogps_solubility":"1.52e-04 g/l","alogps_logp":"7.98","alogps_logs":"-6.45","acceptor_count":"1","donor_count":"1","rotatable_bond_count":"5","polar_surface_area":"20.23","refractivity":"133.6947","polarizability":"55.820822686353566","formal_charge":"0","physiological_charge":"0","pka_strongest_basic":"-0.806973642323843","pka_strongest_acidic":"19.553786825962863","bioavailability":"1","number_of_rings":"4","rule_of_five":"0","ghose_filter":"0","veber_rule":"1","mddr_like_rule":"0","synonyms":["24,25-Dihydrolanosterol","Lanostenol"],"pathways":[{"name":"Steroid biosynthesis","kegg_map_id":"00100"}],"growth_conditions":[],"references":[{"pubmed_id":21062828,"citation":"Scheer, M., Grote, A., Chang, A., Schomburg, I., Munaretto, C., Rother, M., Sohngen, C., Stelzer, M., Thiele, J., Schomburg, D. (2011). \"BRENDA, the enzyme information system in 2011.\" Nucleic Acids Res 39:D670-D676."},{"pubmed_id":1872829,"citation":"Aoyama, Y., Yoshida, Y. (1991). \"Different substrate specificities of lanosterol 14a-demethylase (P-45014DM) of Saccharomyces cerevisiae and rat liver for 24-methylene-24,25-dihydrolanosterol and 24,25-dihydrolanosterol.\" Biochem Biophys Res Commun 178:1064-1071."},{"pubmed_id":1567403,"citation":"Aoyama, Y., Yoshida, Y. (1992). \"The 4 beta-methyl group of substrate does not affect the activity of lanosterol 14 alpha-demethylase (P-450(14)DM) of yeast: difference between the substrate recognition by yeast and plant sterol 14 alpha-demethylases.\" Biochem Biophys Res Commun 183:1266-1272."}],"proteins":[{"created_at":"2011-05-24T20:03:33.000Z","updated_at":"2011-05-27T14:55:59.000Z","name":"Lanosterol 14-alpha demethylase","uniprot_id":"P10614","uniprot_name":"CP51_YEAST","enzyme":true,"transporter":false,"gene_name":"ERG11","num_residues":530,"molecular_weight":"60719.80078","theoretical_pi":"8.95","general_function":"Involved in iron ion binding","specific_function":"Catalyzes C14-demethylation of lanosterol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol","reactions":[{"id":2295,"direction":"\u003e","locations":"Membrane; Single-pass membrane protein","altext":"Obtusifoliol + 3 O(2) + 3 NADPH = 4-alpha-methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3 NADP(+) + 4 H(2)O.","export":false,"pw_reaction_id":null,"source":null},{"id":14387,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006897","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"21-41","pdb_id":null,"cellular_location":"Membrane; Single-pass membrane protein","genbank_gene_id":"M18109","genbank_protein_id":"170946","gene_card_id":"ERG11","chromosome_location":"chromosome 8","locus":"YHR007C","synonyms":["CYPLI","Cytochrome P450 51","Cytochrome P450-14DM","Cytochrome P450-LIA1","Sterol 14-alpha demethylase"],"enzyme_classes":["1.14.13.70"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" heme binding"},{"category":"Function","description":" electron carrier activity"},{"category":"Function","description":" monooxygenase activity"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" ion binding"},{"category":"Function","description":" cation binding"},{"category":"Function","description":" metal ion binding"},{"category":"Function","description":" transition metal ion binding"},{"category":"Function","description":" iron ion binding"},{"category":"Function","description":" oxidoreductase activity"},{"category":"Process","description":" Not Available"}],"pfams":[{"name":"p450","identifier":"PF00067"}],"pathways":[{"name":"Steroid biosynthesis","kegg_map_id":"00100"},{"name":"Cholesterol biosynthesis and metabolism CE(10:0)","kegg_map_id":null},{"name":"Cholesterol biosynthesis and metabolism CE(12:0)","kegg_map_id":null},{"name":"Cholesterol biosynthesis and metabolism CE(14:0)","kegg_map_id":null},{"name":"Cholesterol biosynthesis and metabolism CE(16:0)","kegg_map_id":null},{"name":"Cholesterol biosynthesis and metabolism CE(18:0)","kegg_map_id":null}],"gene_sequence":"ATGTCTGCTACCAAGTCAATCGTTGGAGAGGCATTGGAATACGTAAACATTGGTTTAAGTCATTTCTTGGCTTTACCATTGGCCCAAAGAATCTCTTTGATCATAATAATTCCTTTCATTTACAATATTGTATGGCAATTACTATATTCTTTGAGAAAGGACCGTCCACCTCTAGTGTTTTACTGGATTCCATGGGTCGGTAGTGCTGTTGTGTACGGTATGAAGCCATACGAGTTTTTCGAAGAATGTCAAAAGAAATACGGTGATATTTTTTCATTCGTTTTGTTAGGAAGAGTCATGACTGTGTATTTAGGACCAAAGGGTCACGAATTTGTCTTCAACGCTAAGTTGGCAGATGTTTCAGCAGAAGCTGCTTACGCTCATTTGACTACTCCAGTTTTCGGTAAAGGTGTTATTTACGATTGTCCAAATTCTAGATTGATGGAGCAAAAGAAGTTTGTTAAGGGTGCTCTAACCAAAGAAGCCTTCAAGAGCTACGTTCCATTGATTGCTGAAGAAGTGTACAAGTACTTCAGAGACTCCAAAAACTTCCGTTTGAATGAAAGAACTACTGGTACTATTGACGTGATGGTTACTCAACCTGAAATGACTATTTTCACCGCTTCAAGATCATTATTGGGTAAGGAAATGAGAGCAAAATTGGATACCGATTTTGCTTACTTGTACAGTGATTTGGATAAGGGTTTCACTCCAATCAACTTCGTCTTCCCTAACTTACCATTGGAACACTATAGAAAGAGAGATCACGCTCAAAAGGCTATCTCCGGTACTTACATGTCTTTGATTAAGGAAAGAAGAAAGAACAACGACATTCAAGACAGAGATTTGATCGATTCCTTGATGAAGAACTCTACCTACAAGGATGGTGTGAAGATGACTGATCAAGAAATCGCTAACTTGTTAATTGGTGTCTTAATGGGTGGTCAACATACTTCTGCTGCCACTTCTGCTTGGATTTTGTTGCACTTGGCTGAAAGACCAGATGTCCAACAAGAATTGTACGAAGAACAAATGCGTGTTTTGGATGGTGGTAAGAAGGAATTGACCTACGATTTATTACAAGAAATGCCATTGTTGAACCAAACTATTAAGGAAACTCTAAGAATGCACCATCCATTGCACTCTTTGTTCCGTAAGGTTATGAAAGATATGCACGTTCCAAACACTTCTTATGTCATCCCAGCAGGTTATCACGTTTTGGTTTCTCCAGGTTACACTCATTTAAGAGACGAATACTTCCCTAATGCTCACCAATTCAACATTCACCGTTGGAACAAAGATTCTGCCTCCTCTTATTCCGTCGGTGAAGAAGTCGATTACGGTTTCGGTGCCATTTCTAAGGGTGTCAGCTCTCCATACTTACCTTTCGGTGGTGGTAGACACAGATGTATCGGTGAACACTTTGCTTACTGTCAGCTAGGTGTTCTAATGTCCATTTTTATCAGAACATTAAAATGGCATTACCCAGAGGGTAAGACCGTTCCACCTCCTGACTTTACATCTATGGTTACTCTTCCAACCGGTCCAGCCAAGATCATCTGGGAAAAGAGAAATCCAGAACAAAAGATCTAA","protein_sequence":"MSATKSIVGEALEYVNIGLSHFLALPLAQRISLIIIIPFIYNIVWQLLYSLRKDRPPLVFYWIPWVGSAVVYGMKPYEFFEECQKKYGDIFSFVLLGRVMTVYLGPKGHEFVFNAKLADVSAEAAYAHLTTPVFGKGVIYDCPNSRLMEQKKFVKGALTKEAFKSYVPLIAEEVYKYFRDSKNFRLNERTTGTIDVMVTQPEMTIFTASRSLLGKEMRAKLDTDFAYLYSDLDKGFTPINFVFPNLPLEHYRKRDHAQKAISGTYMSLIKERRKNNDIQDRDLIDSLMKNSTYKDGVKMTDQEIANLLIGVLMGGQHTSAATSAWILLHLAERPDVQQELYEEQMRVLDGGKKELTYDLLQEMPLLNQTIKETLRMHHPLHSLFRKVMKDMHVPNTSYVIPAGYHVLVSPGYTHLRDEYFPNAHQFNIHRWNKDSASSYSVGEEVDYGFGAISKGVSSPYLPFGGGRHRCIGEHFAYCQLGVLMSIFIRTLKWHYPEGKTVPPPDFTSMVTLPTGPAKIIWEKRNPEQKI"}]}