{"ymdb_id":"YMDB00812","created_at":"2011-05-29T18:55:07.000Z","updated_at":"2016-09-08T18:35:56.000Z","name":"acrolein","cas":"107-02-8","state":"Liquid","melting_point":"-87.7 oC","description":"Acrolein (propenal) is the simplest unsaturated aldehyde. It is produced widely but is most often immediately reacted with other products due to its instability and toxicity. Acrolein is a potent inhibitor of yeast alcohol dehydrogenase. It has a piercing, disagreeable, acrid smell similar to that of burning fat. It is responsible for cauliflower-like aromas as a result of bacterial spoilage. [PMID: 10092940]","experimental_water_solubility":"212 mg/mL at 25 oC [SEIDELL,A (1941)]","experimental_logp_hydrophobicity":"-0.01 [HANSCH,C ET AL. (1995)]","location":null,"synthesis_reference":null,"chebi_id":"15368","hmdb_id":null,"kegg_id":"C01471","pubchem_id":"7847","cs_id":"7559","foodb_id":null,"wikipedia_link":"Acrolein","biocyc_id":null,"iupac":"prop-2-enal","traditional_iupac":"acrolein","logp":"0.37433104033333325","pka":null,"alogps_solubility":"1.07e+02 g/l","alogps_logp":"0.18","alogps_logs":"0.28","acceptor_count":"1","donor_count":"0","rotatable_bond_count":"1","polar_surface_area":"17.07","refractivity":"16.366","polarizability":"5.579617832379615","formal_charge":"0","physiological_charge":"0","pka_strongest_basic":"-4.306968103107292","pka_strongest_acidic":null,"bioavailability":"1","number_of_rings":"0","rule_of_five":"1","ghose_filter":"0","veber_rule":"1","mddr_like_rule":"0","synonyms":["2-Propen-1-one","2-Propenal","2-Propenaldehyde","Acquinite","Acraldehyde","Acraldehydeacroleina","Acrolein","Acroleina","Acroleine","Acrylaldehyd","Acrylaldehyde","Acrylic Aldehyde","Akrolein","Akroleina","Aldehyde acrylique","Aldeide acrilica","Allyl aldehyde","Aqualin","Aqualine","Biocide","Crolean","Ethylene aldehyde","Magnacide","Magnacide H","Prop-2-En-1-al","Propenal","Propylene aldehyde","Slimicide","trans-Acrolein"],"pathways":[],"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":18563599,"citation":"Kwolek-Mirek, M., Bednarska, S., Bartosz, G., Bilinski, T. (2009). \"Acrolein toxicity involves oxidative stress caused by glutathione depletion in the yeast Saccharomyces cerevisiae.\" Cell Biol Toxicol 25:363-378."},{"pubmed_id":20971184,"citation":"Ouyang, X., Tran, Q. T., Goodwin, S., Wible, R. S., Sutter, C. H., Sutter, T. R. (2011). \"Yap1 activation by H2O2 or thiol-reactive chemicals elicits distinct adaptive gene responses.\" Free Radic Biol Med 50:1-13."},{"pubmed_id":16820484,"citation":"Trotter, E. W., Collinson, E. J., Dawes, I. W., Grant, C. M. (2006). \"Old yellow enzymes protect against acrolein toxicity in the yeast Saccharomyces cerevisiae.\" Appl Environ Microbiol 72:4885-4892."},{"pubmed_id":7758153,"citation":"Wonisch, W., Schaur, R. J., Bilinski, T., Esterbauer, H. (1995). \"Assessment of growth inhibition by aldehydic lipid peroxidation products and related aldehydes by Saccharomyces cerevisiae.\" Cell Biochem Funct 13:91-98."}],"proteins":[{"created_at":"2011-05-27T07:19:56.000Z","updated_at":"2011-05-27T15:01:27.000Z","name":"NADPH dehydrogenase 2","uniprot_id":"Q03558","uniprot_name":"OYE2_YEAST","enzyme":true,"transporter":false,"gene_name":"OYE2","num_residues":400,"molecular_weight":"45010.39844","theoretical_pi":"6.53","general_function":"Involved in catalytic activity","specific_function":"Oxidizes beta-NADH, beta-NADPH, and alpha-NADPH","reactions":[{"id":2808,"direction":"\u003e","locations":"","altext":"NADPH + acceptor = NADP(+) + reduced acceptor.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":"1OYC","cellular_location":null,"genbank_gene_id":"L06124","genbank_protein_id":"172030","gene_card_id":"OYE2","chromosome_location":"chromosome 8","locus":"YHR179W","synonyms":["Old yellow enzyme 2"],"enzyme_classes":["1.6.99.1"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" nucleotide binding"},{"category":"Function","description":" FMN binding"},{"category":"Function","description":" oxidoreductase activity"},{"category":"Process","description":" metabolic process"}],"pfams":[{"name":"Oxidored_FMN","identifier":"PF00724"}],"pathways":[],"gene_sequence":"ATGCCATTTGTTAAGGACTTTAAGCCACAAGCTTTGGGTGACACCAACTTATTCAAACCAATCAAAATTGGTAACAATGAACTTCTACACCGTGCTGTCATTCCTCCATTGACTAGAATGAGAGCCCAACATCCAGGTAATATTCCAAACAGAGACTGGGCCGTTGAATACTACGCTCAACGTGCTCAAAGACCAGGAACCTTGATTATCACTGAAGGTACCTTTCCCTCTCCACAATCTGGGGGTTACGACAATGCTCCAGGTATCTGGTCCGAAGAACAAATTAAAGAATGGACCAAGATTTTCAAGGCTATTCATGAGAATAAATCGTTCGCATGGGTCCAATTATGGGTTCTAGGTTGGGCTGCTTTCCCAGACACCCTTGCTAGGGATGGTTTGCGTTACGACTCCGCTTCTGACAACGTGTATATGAATGCAGAACAAGAAGAAAAGGCTAAGAAGGCTAACAACCCACAACACAGTATAACAAAGGATGAAATTAAGCAATACGTCAAAGAATACGTCCAAGCTGCCAAAAACTCCATTGCTGCTGGTGCCGATGGTGTTGAAATCCACAGCGCTAACGGTTACTTGTTGAACCAGTTCTTGGACCCACACTCCAATAACAGAACCGATGAGTATGGTGGATCCATCGAAAACAGAGCCCGTTTCACCTTGGAAGTGGTTGATGCAGTTGTCGATGCTATTGGCCCTGAAAAAGTCGGTTTGAGATTGTCTCCATATGGTGTCTTCAACAGTATGTCTGGTGGTGCTGAAACCGGTATTGTTGCTCAATATGCTTATGTCTTAGGTGAACTAGAAAGAAGAGCTAAAGCTGGCAAGCGTTTGGCTTTCGTCCATCTAGTTGAACCTCGTGTCACCAACCCATTTTTAACTGAAGGTGAAGGTGAATACAATGGAGGTAGCAACAAATTTGCTTATTCTATCTGGAAGGGCCCAATTATTAGAGCTGGTAACTTTGCTCTGCACCCAGAAGTTGTCAGAGAAGAGGTGAAGGATCCTAGAACATTGATCGGTTACGGTAGATTTTTTATCTCTAATCCAGATTTGGTTGATCGTTTGGAAAAAGGGTTACCATTAAACAAATATGACAGAGACACTTTCTACAAAATGTCAGCTGAGGGATACATTGACTACCCTACGTACGAAGAAGCTCTAAAACTCGGTTGGGACAAAAATTAA","protein_sequence":"MPFVKDFKPQALGDTNLFKPIKIGNNELLHRAVIPPLTRMRAQHPGNIPNRDWAVEYYAQRAQRPGTLIITEGTFPSPQSGGYDNAPGIWSEEQIKEWTKIFKAIHENKSFAWVQLWVLGWAAFPDTLARDGLRYDSASDNVYMNAEQEEKAKKANNPQHSITKDEIKQYVKEYVQAAKNSIAAGADGVEIHSANGYLLNQFLDPHSNNRTDEYGGSIENRARFTLEVVDAVVDAIGPEKVGLRLSPYGVFNSMSGGAETGIVAQYAYVLGELERRAKAGKRLAFVHLVEPRVTNPFLTEGEGEYNGGSNKFAYSIWKGPIIRAGNFALHPEVVREEVKDPRTLIGYGRFFISNPDLVDRLEKGLPLNKYDRDTFYKMSAEGYIDYPTYEEALKLGWDKN"},{"created_at":"2011-05-27T07:21:51.000Z","updated_at":"2011-05-27T15:01:27.000Z","name":"NADPH dehydrogenase 3","uniprot_id":"P41816","uniprot_name":"OYE3_YEAST","enzyme":true,"transporter":false,"gene_name":"OYE3","num_residues":400,"molecular_weight":"44920.10156","theoretical_pi":"5.31","general_function":"Involved in catalytic activity","specific_function":"Oxidizes beta-NADH, beta-NADPH, and alpha-NADPH","reactions":[{"id":2808,"direction":"\u003e","locations":"","altext":"NADPH + acceptor = NADP(+) + reduced acceptor.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":null,"genbank_gene_id":"L29279","genbank_protein_id":"460039","gene_card_id":"OYE3","chromosome_location":"chromosome 16","locus":"YPL171C","synonyms":["Old yellow enzyme 3"],"enzyme_classes":["1.6.99.1"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" nucleotide binding"},{"category":"Function","description":" FMN binding"},{"category":"Function","description":" oxidoreductase activity"},{"category":"Process","description":" metabolic process"}],"pfams":[{"name":"Oxidored_FMN","identifier":"PF00724"}],"pathways":[],"gene_sequence":"ATGCCATTTGTAAAAGGTTTTGAGCCGATCTCCCTAAGAGACACAAACCTTTTTGAACCAATTAAGATTGGTAACACTCAGCTTGCACATCGTGCGGTTATGCCCCCATTGACCAGAATGAGGGCCACTCACCCCGGAAATATTCCAAATAAGGAGTGGGCTGCTGTGTATTATGGTCAGCGTGCTCAAAGACCTGGTACCATGATCATCACGGAAGGTACGTTTATTTCCCCTCAAGCCGGCGGCTATGACAACGCCCCTGGGATTTGGTCTGATGAGCAGGTCGCTGAGTGGAAGAATATCTTTTTAGCCATCCATGATTGTCAGTCGTTCGCGTGGGTACAACTTTGGTCTTTAGGCTGGGCATCCTTCCCAGACGTATTGGCAAGAGACGGGTTACGCTATGACTGTGCATCTGACAGAGTGTATATGAATGCTACGTTACAAGAAAAGGCCAAAGATGCGAATAATCTCGAACATAGTTTGACTAAAGACGACATTAAACAGTATATCAAGGATTACATCCATGCGGCTAAGAATTCTATCGCGGCTGGCGCCGATGGTGTAGAAATTCATAGCGCCAATGGGTACTTGTTGAATCAGTTCTTGGATCCACATTCTAATAAGAGGACCGACGAATACGGCGGAACGATCGAAAACAGGGCCCGCTTTACACTGGAGGTTGTCGATGCTCTTATCGAAACTATCGGTCCTGAACGGGTGGGTTTGAGGTTGTCGCCGTACGGCACTTTTAACAGTATGTCTGGGGGTGCTGAACCAGGTATTATCGCTCAATATTCGTATGTTTTGGGTGAATTAGAGAAGAGGGCAAAGGCTGGTAAGCGTTTGGCCTTTGTGCACCTCGTTGAACCACGTGTCACGGACCCATCGTTGGTGGAGGGCGAAGGAGAATATTCCGAGGGTACTAACGATTTTGCCTACTCTATATGGAAGGGTCCAATCATCAGAGCTGGTAATTACGCTCTTCATCCAGAAGTGGTTAGAGAACAAGTAAAGGATCCCAGAACCTTGATAGGCTATGGTAGATTCTTCATCTCTAACCCAGATTTAGTCTACCGTTTAGAAGAGGGCCTGCCATTGAACAAGTATGACAGAAGTACCTTCTACACCATGTCCGCGGAAGGTTATACCGACTACCCAACATATGAAGAGGCAGTAGATTTAGGTTGGAACAAGAACTGA","protein_sequence":"MPFVKGFEPISLRDTNLFEPIKIGNTQLAHRAVMPPLTRMRATHPGNIPNKEWAAVYYGQRAQRPGTMIITEGTFISPQAGGYDNAPGIWSDEQVAEWKNIFLAIHDCQSFAWVQLWSLGWASFPDVLARDGLRYDCASDRVYMNATLQEKAKDANNLEHSLTKDDIKQYIKDYIHAAKNSIAAGADGVEIHSANGYLLNQFLDPHSNKRTDEYGGTIENRARFTLEVVDALIETIGPERVGLRLSPYGTFNSMSGGAEPGIIAQYSYVLGELEKRAKAGKRLAFVHLVEPRVTDPSLVEGEGEYSEGTNDFAYSIWKGPIIRAGNYALHPEVVREQVKDPRTLIGYGRFFISNPDLVYRLEEGLPLNKYDRSTFYTMSAEGYTDYPTYEEAVDLGWNKN"}]}