{"ymdb_id":"YMDB00395","created_at":"2011-05-29T18:12:29.000Z","updated_at":"2016-09-08T18:35:26.000Z","name":"Palmitaldehyde","cas":"629-80-1","state":"Solid","melting_point":"35 oC","description":"Palmitaldehyde is an intermediate in the metabolism of glycosphingolipid. It is a substrate for sphingosine-1-phosphate lyase 1.","experimental_water_solubility":"","experimental_logp_hydrophobicity":"","location":"extracellular;cell envelope;mitochondrion;lipid particle;endoplasmic reticulum","synthesis_reference":"Vignais, Pierce V.; Zabin, Irving.  Formation of palmitaldehyde in rat brain.    Biochem. Lipids Proc. 5th Intern. Conf. Vienna  (1960),  Volume Date 1958,     78-84. ","chebi_id":"17600","hmdb_id":"HMDB01551","kegg_id":"C00517","pubchem_id":"984","cs_id":"959","foodb_id":null,"wikipedia_link":null,"biocyc_id":"PALMITALDEHYDE","iupac":"hexadecanal","traditional_iupac":"palmitoyl","logp":"6.097966525333334","pka":null,"alogps_solubility":"5.88e-05 g/l","alogps_logp":"7.18","alogps_logs":"-6.61","acceptor_count":"1","donor_count":"0","rotatable_bond_count":"14","polar_surface_area":"17.07","refractivity":"76.1582","polarizability":"33.38660774965068","formal_charge":"0","physiological_charge":"0","pka_strongest_basic":"-6.944305999531455","pka_strongest_acidic":"15.55551402037299","bioavailability":"0","number_of_rings":"0","rule_of_five":"0","ghose_filter":"0","veber_rule":"0","mddr_like_rule":"0","synonyms":["Palmitaldehyde","palmitoyl aldehyde"],"pathways":[{"name":"Fatty acid metabolism","kegg_map_id":"00071"},{"name":"Sphingolipid metabolism","kegg_map_id":"00600"}],"growth_conditions":[],"references":[{"pubmed_id":21051339,"citation":"UniProt Consortium (2011). \"Ongoing and future developments at the Universal Protein Resource.\" Nucleic Acids Res 39:D214-D219."},{"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":18846089,"citation":"Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). \"A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology.\" Nat Biotechnol 26:1155-1160."},{"pubmed_id":10900202,"citation":"Mao, C., Xu, R., Bielawska, A., Szulc, Z. M., Obeid, L. M. (2000). \"Cloning and characterization of a Saccharomyces cerevisiae alkaline ceramidase with specificity for dihydroceramide.\" J Biol Chem 275:31369-31378."},{"pubmed_id":12531550,"citation":"Obeid, L. M., Okamoto, Y., Mao, C. (2002). \"Yeast sphingolipids: metabolism and biology.\" Biochim Biophys Acta 1585:163-171."}],"proteins":[{"created_at":"2011-05-27T02:15:17.000Z","updated_at":"2011-05-27T15:01:17.000Z","name":"Sphingosine-1-phosphate lyase","uniprot_id":"Q05567","uniprot_name":"SGPL_YEAST","enzyme":true,"transporter":false,"gene_name":"DPL1","num_residues":589,"molecular_weight":"65565.10156","theoretical_pi":"8.15","general_function":"Involved in carboxy-lyase activity","specific_function":"Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine","reactions":[{"id":1895,"direction":"\u003e","locations":"endoplasmic reticulum","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1972,"direction":"\u003e","locations":"endoplasmic reticulum","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2666,"direction":"\u003e","locations":null,"altext":"Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":null,"genbank_gene_id":"U51031","genbank_protein_id":"1230658","gene_card_id":"DPL1","chromosome_location":"chromosome 4","locus":"YDR294C","synonyms":["SP-lyase","ySPL","Bestowed of sphingosine tolerance 1","Sphingosine-1-phosphate aldolase"],"enzyme_classes":["4.1.2.27"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" lyase activity"},{"category":"Function","description":" carbon-carbon lyase activity"},{"category":"Function","description":" carboxy-lyase activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" cofactor binding"},{"category":"Function","description":" pyridoxal phosphate binding"},{"category":"Function","description":" catalytic activity"},{"category":"Process","description":" cellular metabolic process"},{"category":"Process","description":" organic acid metabolic process"},{"category":"Process","description":" oxoacid metabolic process"},{"category":"Process","description":" carboxylic acid metabolic process"},{"category":"Process","description":" metabolic process"}],"pfams":[{"name":"Pyridoxal_deC","identifier":"PF00282"}],"pathways":[{"name":"Sphingolipid metabolism","kegg_map_id":"00600"}],"gene_sequence":"ATGAGTGGAGTATCAAATAAAACAGTATCAATTAATGGTTGGTATGGCATGCCAATTCATTTACTAAGGGAAGAAGGCGACTTTGCCCAGTTTATGATTCTAACCATCAACGAATTAAAAATAGCCATACATGGTTACCTCAGAAATACCCCATGGTACAACATGTTGAAGGATTATTTGTTTGTGATCTTTTGTTACAAGCTAATAAGTAATTTTTTTTATCTGTTGAAAGTTTATGGGCCGGTGAGGTTAGCAGTGAGAACATACGAGCATAGTTCCAGAAGATTGTTTCGTTGGTTATTGGACTCACCATTTTTGAGGGGTACCGTAGAAAAGGAAGTCACAAAGGTCAAACAATCGATCGAAGACGAACTAATTAGATCGGACTCTCAGTTAATGAATTTCCCACAGTTGCCATCCAATGGGATACCTCAGGATGATGTTATTGAAGAGCTAAATAAATTGAACGACTTGATACCACATACCCAATGGAAGGAAGGAAAGGTCTCTGGTGCCGTTTACCACGGTGGTGATGATTTGATCCACTTACAAACAATCGCATACGAAAAATATTGCGTTGCCAATCAATTACATCCCGATGTCTTTCCTGCCGTACGTAAAATGGAATCCGAAGTGGTTTCTATGGTTTTAAGAATGTTTAATGCCCCTTCTGATACAGGTTGTGGTACCACAACTTCAGGTGGTACAGAATCCTTGCTTTTAGCATGTCTGAGCGCTAAAATGTATGCCCTTCATCATCGTGGAATCACCGAACCAGAAATAATTGCTCCCGTAACTGCACATGCTGGGTTTGACAAAGCTGCTTATTACTTTGGCATGAAGCTACGCCACGTGGAGCTAGATCCAACGACATATCAAGTGGACCTGGGAAAAGTGAAAAAATTCATCAATAAGAACACAATTTTACTGGTCGGTTCCGCTCCAAACTTTCCTCATGGTATTGCCGATGATATTGAAGGATTGGGTAAAATAGCACAAAAATATAAACTTCCTTTACACGTCGACAGTTGTCTAGGTTCCTTTATTGTTTCATTTATGGAAAAGGCTGGTTACAAAAATCTGCCATTACTTGACTTTAGAGTCCCGGGAGTCACCTCAATATCATGTGACACTCATAAATATGGATTTGCACCAAAAGGCTCGTCAGTTATAATGTATAGAAACAGCGACTTACGAATGCATCAGTATTACGTAAATCCTGCTTGGACTGGCGGGTTATATGGCTCTCCTACATTAGCAGGGTCCAGGCCTGGTGCTATTGTCGTAGGTTGTTGGGCCACTATGGTCAACATGGGTGAAAATGGGTACATTGAGTCGTGCCAAGAAATAGTCGGTGCAGCAATGAAGTTTAAAAAATACATCCAGGAAAACATTCCAGACCTGAATATAATGGGCAACCCTAGATATTCAGTCATTTCATTTTCTTCAAAGACCTTGAACATACACGAACTATCTGACAGGTTGTCCAAGAAAGGCTGGCATTTCAATGCCCTACAAAAGCCGGTTGCACTACACATGGCCTTCACGAGATTGAGCGCTCATGTTGTGGATGAGATCTGCGACATTTTACGTACTACCGTGCAAGAGTTGAAGAGCGAATCAAATTCTAAACCATCCCCAGACGGAACTAGCGCTCTATATGGTGTCGCCGGGAGCGTTAAAACTGCTGGCGTTGCAGACAAATTGATTGTGGGATTCCTAGACGCATTATACAAGTTGGGTCCAGGAGAGGATACCGCCACCAAGTAG","protein_sequence":"MSGVSNKTVSINGWYGMPIHLLREEGDFAQFMILTINELKIAIHGYLRNTPWYNMLKDYLFVIFCYKLISNFFYLLKVYGPVRLAVRTYEHSSRRLFRWLLDSPFLRGTVEKEVTKVKQSIEDELIRSDSQLMNFPQLPSNGIPQDDVIEELNKLNDLIPHTQWKEGKVSGAVYHGGDDLIHLQTIAYEKYCVANQLHPDVFPAVRKMESEVVSMVLRMFNAPSDTGCGTTTSGGTESLLLACLSAKMYALHHRGITEPEIIAPVTAHAGFDKAAYYFGMKLRHVELDPTTYQVDLGKVKKFINKNTILLVGSAPNFPHGIADDIEGLGKIAQKYKLPLHVDSCLGSFIVSFMEKAGYKNLPLLDFRVPGVTSISCDTHKYGFAPKGSSVIMYRNSDLRMHQYYVNPAWTGGLYGSPTLAGSRPGAIVVGCWATMVNMGENGYIESCQEIVGAAMKFKKYIQENIPDLNIMGNPRYSVISFSSKTLNIHELSDRLSKKGWHFNALQKPVALHMAFTRLSAHVVDEICDILRTTVQELKSESNSKPSPDGTSALYGVAGSVKTAGVADKLIVGFLDALYKLGPGEDTATK"}]}