{"ymdb_id":"YMDB00339","created_at":"2011-05-29T18:07:37.000Z","updated_at":"2016-09-08T18:35:22.000Z","name":"N1-Acetylspermine","cas":"25593-72-0","state":"Solid","melting_point":null,"description":"N1-Acetylspermine is an intermediate in spermine and spermidine degradation pathway. Polyamines (e.g. spermidine, putrescine, spermine) are a ubiquitous group of compounds involved in many biological processes, including binding to nucleic acids, stabilizing membranes, and stimulating several enzymes. [Biocyc POLYAMINSYN3-PWY and PWY-6117] ","experimental_water_solubility":null,"experimental_logp_hydrophobicity":null,"location":"cytoplasm","synthesis_reference":null,"chebi_id":"17312","hmdb_id":"HMDB01186","kegg_id":"C02567","pubchem_id":"916","cs_id":"892","foodb_id":null,"wikipedia_link":null,"biocyc_id":"N1-ACETYLSPERMINE","iupac":"N-[3-({4-[(3-aminopropyl)amino]butyl}amino)propyl]acetamide","traditional_iupac":"N(1)-acetylspermine","logp":"-1.6351610130000012","pka":null,"alogps_solubility":"3.71e-01 g/l","alogps_logp":"-0.42","alogps_logs":"-2.82","acceptor_count":"4","donor_count":"4","rotatable_bond_count":"12","polar_surface_area":"79.17999999999999","refractivity":"72.002","polarizability":"30.67903315909775","formal_charge":"0","physiological_charge":"3","pka_strongest_basic":"10.79088463554729","pka_strongest_acidic":"16.295172537507565","bioavailability":"1","number_of_rings":"0","rule_of_five":"1","ghose_filter":"0","veber_rule":"0","mddr_like_rule":"0","synonyms":["N-(3-((4-((3-aminopropyl)amino)butyl)amino)propyl)-Acetamide","N-Acetylspermine","N'-Acetylspermine","N'-Monoacetylspermine","N(1)-Acetylspermine","N1-Acetylspermine"],"pathways":[],"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."}],"proteins":[{"created_at":"2011-05-24T21:12:40.000Z","updated_at":"2011-05-27T15:00:57.000Z","name":"Polyamine oxidase FMS1","uniprot_id":"P50264","uniprot_name":"FMS1_YEAST","enzyme":true,"transporter":false,"gene_name":"FMS1","num_residues":508,"molecular_weight":"57805.10156","theoretical_pi":"5.38","general_function":"Amino acid transport and metabolism","specific_function":"Involved in the production of beta-alanine, a precursor of pantothenic acid. Multicopy suppressor of fenpropimorph resistance","reactions":[{"id":1903,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1906,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1907,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2368,"direction":"\u003e","locations":null,"altext":"Spermine + O(2) + H(2)O = spermidine + 3-aminopropanal + H(2)O(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2369,"direction":"\u003e","locations":null,"altext":"Spermidine + O(2) + H(2)O = putrescine + 3-aminopropanal + H(2)O(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2370,"direction":"\u003e","locations":null,"altext":"N(1)-acetylspermine + O(2) + H(2)O = spermidine + 3-acetamidopropanal + H(2)O(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2371,"direction":"\u003e","locations":null,"altext":"N(1)-acetylspermidine + O(2) + H(2)O = putrescine + 3-acetamidopropanal + H(2)O(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2372,"direction":"\u003e","locations":null,"altext":"N(8)-acetylspermidine + O(2) + H(2)O = 4-acetamidobutanal + trimethylenediamine + H(2)O(2).","export":false,"pw_reaction_id":null,"source":null},{"id":3757,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006281","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":"1YY5","cellular_location":null,"genbank_gene_id":"X81848","genbank_protein_id":"1143556","gene_card_id":"FMS1","chromosome_location":"chromosome 13","locus":"YMR020W","synonyms":["Fenpropimorph resistance multicopy suppressor 1"],"enzyme_classes":["1.5.3.17"],"go_classes":[],"pfams":[{"name":"Amino_oxidase","identifier":"PF01593"}],"pathways":[{"name":"beta-Alanine metabolism","kegg_map_id":"00410"}],"gene_sequence":"ATGAATACAGTTTCACCAGCCAAAAAAAAGGTTATTATAATTGGTGCCGGTATTGCTGGGCTTAAAGCTGCATCTACGCTACACCAAAACGGTATTCAAGATTGTCTTGTTCTTGAGGCCAGAGATCGGGTCGGTGGTAGGTTGCAAACTGTCACAGGCTATCAAGGTCGGAAATATGATATAGGTGCTAGCTGGCACCATGATACGTTGACAAACCCTTTATTTTTGGAAGAGGCTCAACTGAGTTTGAATGATGGGAGAACGAGGTTTGTTTTTGATGACGATAATTTTATTTATATCGACGAAGAACGTGGAAGGGTAGACCATGACAAGGAACTGCTTCTTGAAATTGTGGACAATGAAATGAGCAAATTCGCAGAGTTAGAATTCCATCAACACTTAGGAGTTTCAGATTGCTCCTTTTTTCAATTAGTAATGAAATACTTACTACAAAGACGCCAATTTCTCACAAATGACCAAATAAGATATTTGCCACAACTCTGTCGATATCTGGAATTGTGGCACGGCTTAGATTGGAAGCTTTTGAGTGCCAAGGATACATACTTCGGTCACCAAGGAAGGAACGCCTTTGCTTTGAACTATGATTCTGTGGTTCAAAGAATTGCTCAAAGCTTTCCTCAAAATTGGTTAAAGCTAAGTTGTGAAGTGAAATCAATTACACGAGAACCTTCAAAAAATGTGACAGTGAACTGTGAAGATGGTACTGTGTACAATGCTGATTATGTTATTATTACAGTACCTCAAAGTGTATTGAATTTGTCTGTACAACCTGAAAAAAATTTACGGGGAAGAATAGAATTTCAACCACCCTTGAAACCAGTGATTCAAGATGCTTTTGACAAGATCCATTTTGGAGCGCTAGGTAAAGTAATTTTTGAGTTTGAAGAATGTTGTTGGTCGAACGAAAGTTCAAAAATTGTAACTTTGGCTAACTCTACCAATGAATTTGTCGAAATAGTACGTAATGCGGAAAATTTAGATGAATTAGACTCTATGCTAGAAAGGGAAGATTCTCAAAAGCATACGAGTGTTACTTGTTGGAGCCAGCCTTTATTTTTCGTAAATTTGTCAAAAAGCACAGGAGTAGCAAGCTTTATGATGTTGATGCAGGCACCGCTTACAAATCACATAGAATCCATTAGAGAAGATAAAGAGCGTCTTTTTAGTTTTTTCCAACCTGTGCTGAACAAGATTATGAAGTGTCTAGATTCTGAGGATGTCATCGACGGAATGAGGCCGATAGAAAACATTGCAAACGCTAATAAACCAGTCTTAAGAAACATCATCGTTAGCAACTGGACACGCGATCCTTACTCACGCGGTGCTTATTCGGCCTGTTTTCCAGGAGATGATCCAGTTGATATGGTTGTTGCAATGTCTAATGGTCAAGACTCCCGCATAAGATTTGCAGGCGAACATACTATCATGGACGGCGCCGGCTGTGCCTATGGTGCTTGGGAAAGCGGAAGACGGGAGGCGACTCGAATCTCTGACTTACTGAAATAG","protein_sequence":"MNTVSPAKKKVIIIGAGIAGLKAASTLHQNGIQDCLVLEARDRVGGRLQTVTGYQGRKYDIGASWHHDTLTNPLFLEEAQLSLNDGRTRFVFDDDNFIYIDEERGRVDHDKELLLEIVDNEMSKFAELEFHQHLGVSDCSFFQLVMKYLLQRRQFLTNDQIRYLPQLCRYLELWHGLDWKLLSAKDTYFGHQGRNAFALNYDSVVQRIAQSFPQNWLKLSCEVKSITREPSKNVTVNCEDGTVYNADYVIITVPQSVLNLSVQPEKNLRGRIEFQPPLKPVIQDAFDKIHFGALGKVIFEFEECCWSNESSKIVTLANSTNEFVEIVRNAENLDELDSMLEREDSQKHTSVTCWSQPLFFVNLSKSTGVASFMMLMQAPLTNHIESIREDKERLFSFFQPVLNKIMKCLDSEDVIDGMRPIENIANANKPVLRNIIVSNWTRDPYSRGAYSACFPGDDPVDMVVAMSNGQDSRIRFAGEHTIMDGAGCAYGAWESGRREATRISDLLK"}]}