{"ymdb_id":"YMDB00042","created_at":"2011-05-29T15:51:00.000Z","updated_at":"2016-09-08T18:34:56.000Z","name":"1,3-Diaminopropane","cas":"109-76-2","state":"Liquid","melting_point":"-12 oC","description":"1,3-Diaminopropane is a polyamine involved in the arginine/proline metabolic pathways and the beta-alanine metabolic pathway.","experimental_water_solubility":"","experimental_logp_hydrophobicity":"-1.43 [HANSCH,C ET AL. (1995)]","location":"cytoplasm","synthesis_reference":"Takayanagi, Yasuyuki; Oohinata, Takahiro.  Preparation of 1,3-diaminopropane from acrylonitrile and ammonia.    Jpn. Kokai Tokkyo Koho  (1994),     5 pp.","chebi_id":"15725","hmdb_id":"HMDB00002","kegg_id":"C00986","pubchem_id":"428","cs_id":"415","foodb_id":null,"wikipedia_link":"1,3-Diaminopropane","biocyc_id":"CPD-313","iupac":"propane-1,3-diamine","traditional_iupac":"α,ω-propanediamine","logp":"-1.362482935","pka":null,"alogps_solubility":"4.37e+02 g/l","alogps_logp":"-1.41","alogps_logs":"0.77","acceptor_count":"2","donor_count":"2","rotatable_bond_count":"2","polar_surface_area":"52.04","refractivity":"22.734","polarizability":"9.059383875573538","formal_charge":"0","physiological_charge":"2","pka_strongest_basic":"10.169241483553524","pka_strongest_acidic":null,"bioavailability":"1","number_of_rings":"0","rule_of_five":"1","ghose_filter":"0","veber_rule":"0","mddr_like_rule":"0","synonyms":["1,3-Diaminepropane","1,3-Diamino-n-propane","1,3-propanediamine","1,3-Propylenediamine","1,3-Trimethylenediamine","3-Aminopropylamine","a,w-Propanediamine","Propane-1,3-diamine","tn","Trimethylenediamine","Trimethylenediamine dihydrochloride","Trimethylenediamine hydrochloride"],"pathways":[{"name":"Arginine and proline metabolism","kegg_map_id":"00330"},{"name":"beta-Alanine metabolism","kegg_map_id":"00410"},{"name":"Glycine, serine and threonine metabolism","kegg_map_id":"00260"}],"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":9163530,"citation":"Abid, M. R., Sasaki, K., Titani, K., Miyazaki, M. (1997). \"Biochemical and immunological characterization of deoxyhypusine synthase purified from the yeast Saccharomyces carlsbergensis.\" J Biochem 121:769-778."}],"proteins":[{"created_at":"2011-05-24T21:12:04.000Z","updated_at":"2011-07-22T17:54:35.000Z","name":"Deoxyhypusine synthase","uniprot_id":"P38791","uniprot_name":"DHYS_YEAST","enzyme":true,"transporter":false,"gene_name":"DYS1","num_residues":387,"molecular_weight":"42891.80078","theoretical_pi":"5.49","general_function":"Involved in peptidyl-lysine modification to hypusine","specific_function":"Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue","reactions":[{"id":1444,"direction":"\u003e","locations":"mitochondrion;mitochondrial membrane;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2367,"direction":"\u003e","locations":null,"altext":"[eIF5A-precursor]-lysine + spermidine = [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":null,"genbank_gene_id":"AY558282","genbank_protein_id":"45270454","gene_card_id":"DYS1","chromosome_location":"chromosome 8","locus":"YHR068W","synonyms":["DHS"],"enzyme_classes":["2.5.1.46"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" Not Available"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" macromolecule metabolic process"},{"category":"Process","description":" macromolecule modification"},{"category":"Process","description":" protein modification process"},{"category":"Process","description":" peptidyl-amino acid modification"},{"category":"Process","description":" peptidyl-lysine modification"},{"category":"Process","description":" peptidyl-lysine modification to hypusine"}],"pfams":[{"name":"DS","identifier":"PF01916"}],"pathways":[],"gene_sequence":"ATGTCCGATATCAACGAAAAACTCCCAGAGTTACTACAAGACGCTGTCTTGAAAGCATCTGTTCCTATTCCAGATGACTTCGTTAAGGTTCAAGGTATTGATTACTCAAAGCCTGAAGCCACTAATATGAGAGCAACTGATTTAATTGAAGCTATGAAGACCATGGGTTTCCAAGCTAGTTCTGTTGGTACTGCCTGTGAGATTATTGATAGTATGAGATCATGGAGAGGTAAGCATATTGACGAATTGGATGACCATGAAAAGAAAGGTTGCTTCGATGAGGAAGGGTACCAAAAGACTACTATCTTCATGGGTTATACTTCTAACTTGATCAGTTCCGGTGTACGTGAAACTTTACGTTATTTGGTGCAACACAAAATGGTTGATGCTGTCGTTACTTCTGCTGGTGGTGTGGAAGAAGATTTGATCAAATGTCTTGCTCCAACTTACTTGGGTGAATTTGCTTTGAAAGGTAAATCTTTGCGTGACCAAGGTATGAATCGTATTGGTAACTTGCTTGTTCCAAATGATAACTACTGTAAGTTTGAAGAATGGATTGTCCCAATTTTGGATAAGATGTTGGAAGAACAAGATGAATACGTAAAGAAACATGGCGCTGACTGTTTAGAGGCTAACCAAGACGTGGATTCACCAATCTGGACCCCATCTAAGATGATAGACCGTTTTGGTAAGGAAATCAACGACGAATCCTCCGTATTGTACTGGGCCCACAAGAATAAAATTCCAATCTTTTGTCCATCTTTGACTGATGGTTCAATCGGTGACATGTTGTTTTTCCATACTTTTAAAGCATCTCCAAAACAACTAAGAGTTGACATTGTAGGAGATATCCGCAAAATCAATTCAATGTCCATGGCCGCTTACAGAGCCGGTATGATCATCTTGGGTGGTGGTTTGATCAAGCACCACATTGCCAATGCTTGTTTGATGAGAAATGGTGCTGATTATGCCGTTTACATTAACACTGGTCAAGAATACGATGGTTCTGATGCAGGTGCAAGACCTGACGAAGCTGTGTCTTGGGGTAAGATCAAGGCTGAAGCCAAATCCGTCAAACTTTTTGCTGATGTCACCACTGTTCTTCCATTGATTGTTGCTGCTACCTTTGCCAGTGGTAAACCAATCAAAAAAGTTAAGAATTGA","protein_sequence":"MSDINEKLPELLQDAVLKASVPIPDDFVKVQGIDYSKPEATNMRATDLIEAMKTMGFQASSVGTACEIIDSMRSWRGKHIDELDDHEKKGCFDEEGYQKTTIFMGYTSNLISSGVRETLRYLVQHKMVDAVVTSAGGVEEDLIKCLAPTYLGEFALKGKSLRDQGMNRIGNLLVPNDNYCKFEEWIVPILDKMLEEQDEYVKKHGADCLEANQDVDSPIWTPSKMIDRFGKEINDESSVLYWAHKNKIPIFCPSLTDGSIGDMLFFHTFKASPKQLRVDIVGDIRKINSMSMAAYRAGMIILGGGLIKHHIANACLMRNGADYAVYINTGQEYDGSDAGARPDEAVSWGKIKAEAKSVKLFADVTTVLPLIVAATFASGKPIKKVKN"},{"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"}]}