BioPAX pathway converted from "S-Adenosyl methionine <=> Decarboxylated-Adenosyl methionine + CO2" in the Reactome database.LEFT-TO-RIGHT4.1.1.50S-Adenosyl methionine <=> Decarboxylated-Adenosyl methionine + CO2S-Adenosylmethionine decarboxylase belongs to a small class of amino acid decarboxylases that use a covalently bound pyruvate as a prosthetic group. It is an essential enzyme for polyamine biosynthesis and provides an important target for the design of anti-parasitic and cancer chemotherapeutic agents. It catalyzes the formation of the aminopropyl group donor in the biosynthesis of the polyamines spermidine and spermine. These pyruvoyl-dependent decarboxylases also form amines such as histamine, decarboxylated S-adenosylmethionine, phosphatidylethanolamine (a component of membrane phospholipids), and -alanine (a precursor of coenzyme A), which are all of critical importance in cellular physiology and provide important targets for drug design.Authored: Gopinathrao, G, 2008-05-21 15:52:50Reviewed: D'Eustachio, P, 2008-06-12 14:43:38Edited: Gopinathrao, G, 2006-04-27 13:13:48SAMAdoMetS-adenosylmethionineS-adenosyl-L-methionineReactome DB_ID: 71284cytosolGENE ONTOLOGYGO:0005829S-adenosyl-L-methionine [ChEBI:15414]S-adenosyl-L-methionineChEBICHEBI:15414Reactome Database ID Release 7571284Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=71284ReactomeR-ALL-712844Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-ALL-71284.4Reactomehttp://www.reactome.orgCOMPOUNDC00019additional informationMIMI:0361SAMdc-AdoMetdecarboxyAdoMetS-adenosylmethioninamineDecarboxylated AdoMetReactome DB_ID: 353113S-adenosylmethioninamine [ChEBI:15625]S-adenosylmethioninamineS--adenosylmethioninamine(5-Deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium saltS-Adenosyl-3-methylthiopropylamine[1-(adenin-9-yl)-1,5-dideoxy-beta-D-ribofuranos-5-yl](3-aminopropyl)(methyl)sulfoniumChEBICHEBI:15625Reactome Database ID Release 75353113Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=353113ReactomeR-ALL-3531135Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-ALL-353113.5CO2carbon dioxideReactome DB_ID: 113528carbon dioxide [ChEBI:16526]carbon dioxideChEBICHEBI:16526Reactome Database ID Release 75113528Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113528ReactomeR-ALL-1135283Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-ALL-113528.3COMPOUNDC00011ACTIVATIONAdoMetDCAMD1(1-67)Reactome DB_ID: 351223UniProt:P17707 AMD1AMD1AMDFUNCTION Essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels.ACTIVITY REGULATION Both proenzyme processing and catalytic activity are stimulated by putrescine. Catalytic activity is inhibited by iodoacetic acid.PATHWAY Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.SUBUNIT Heterotetramer of two alpha and two beta chains.PTM Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.SIMILARITY Belongs to the eukaryotic AdoMetDC family.Homo sapiensNCBI Taxonomy9606UniProtP177071EQUAL67EQUALReactome Database ID Release 75351223Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=351223ReactomeR-HSA-3512231Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-351223.1GENE ONTOLOGYGO:0004014gene ontology term for cellular functionMIMI:0355Same Catalyst ActivityReactome Database ID Release 75351211Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=351211Reactome Database ID Release 75351222Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=351222ReactomeR-HSA-3512221Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-351222.110029540Pubmed1999Role of cysteine-82 in the catalytic mechanism of human S-adenosylmethionine decarboxylaseXiong, HStanley, BAPegg, AEBiochemistry 38:2462-7011583147Pubmed2001The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylaseTolbert, WDEkstrom, JLMathews, IISecrist JA, 3rdKapoor, PPegg, AEEalick, SEBiochemistry 40:9484-94