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Is also able to decarboxylate L-canavanine, although less efficiently. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginine + H(+) = agmatine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17641"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:32682"},{"database":"ChEBI","id":"CHEBI:58145"}],"ecNumber":"4.1.1.19","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18650422"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyruvate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18650422"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:15361"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18650422"}],"value":"Binds 1 pyruvoyl group covalently per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18650422"}],"value":"Highly competitively inhibited by L-argininamide and L-arginine methyl ester. Also inhibited by alpha-difluoromethylarginine. Is not stimulated by potassium chloride as observed for other decarboxylases"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":1.1,"unit":"umol/min/mg","enzyme":"enzyme","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18650422"}]}],"michaelisConstants":[{"constant":150.0,"unit":"uM","substrate":"L-arginine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18650422"}]}]},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18650422"}],"value":"Optimum pH is 6."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18650422"}],"value":"Optimum temperature is 80 degrees Celsius. Highly thermostable. 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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"}],"commentType":"PTM"},{"commentType":"MASS SPECTROMETRY","molecule":"Arginine decarboxylase alpha chain","method":"Electrospray","molWeight":6123.0,"molWeightError":0.0,"note":"Pyruvoyl group-containing alpha subunit.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18650422"}]},{"texts":[{"value":"A chimeric protein containing the beta subunit of SSO0536 and the alpha subunit of SSO0585 (SpeH) has ArgDC activity and no AdoMetDC activity, implicating residues responsible for substrate specificity in the beta subunit. But additional factors in the alpha subunit are required for efficient cleavage and turnover"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"Arginine decarboxylase beta chain","featureId":"PRO_0000030149"},{"type":"Chain","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"Arginine decarboxylase alpha chain","featureId":"PRO_0000030150"},{"type":"Active site","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate; via pyruvic acid","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Active site","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"Proton acceptor; for processing activity","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Active site","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"Proton donor; for catalytic activity","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Site","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"Cleavage (non-hydrolytic); by autolysis"},{"type":"Modified residue","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"Pyruvic acid (Ser); by autocatalysis","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18650422"}]}],"keywords":[{"id":"KW-0068","category":"PTM","name":"Autocatalytic cleavage"},{"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"id":"KW-0620","category":"Biological process","name":"Polyamine biosynthesis"},{"id":"KW-0670","category":"Ligand","name":"Pyruvate"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0704","category":"Ligand","name":"Schiff base"},{"id":"KW-0865","category":"PTM","name":"Zymogen"}],"references":[{"referenceNumber":1,"citation":{"id":"10701121","citationType":"journal article","authors":["Charlebois R.L.","Singh R.K.","Chan-Weiher C.C.-Y.","Allard G.","Chow C.","Confalonieri F.","Curtis B.","Duguet M.","Erauso G.","Faguy D.","Gaasterland T.","Garrett R.A.","Gordon P.","Jeffries A.C.","Kozera C.","Kushwaha N.","Lafleur E.","Medina N.","Peng X.","Penny S.L.","She Q.","St Jean A.","van der Oost J.","Young F.","Zivanovic Y.","Doolittle W.F.","Ragan M.A.","Sensen C.W."],"citationCrossReferences":[{"database":"PubMed","id":"10701121"},{"database":"DOI","id":"10.1139/g99-108"}],"title":"Gene content and organization of a 281-kbp contig from the genome of the extremely thermophilic archaeon, Sulfolobus solfataricus P2.","publicationDate":"2000","journal":"Genome","firstPage":"116","lastPage":"136","volume":"43"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 35092 / DSM 1617 / JCM 11322 / P2","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"11427726","citationType":"journal article","authors":["She Q.","Singh R.K.","Confalonieri F.","Zivanovic Y.","Allard G.","Awayez M.J.","Chan-Weiher C.C.-Y.","Clausen I.G.","Curtis B.A.","De Moors A.","Erauso G.","Fletcher C.","Gordon P.M.K.","Heikamp-de Jong I.","Jeffries A.C.","Kozera C.J.","Medina N.","Peng X.","Thi-Ngoc H.P.","Redder P.","Schenk M.E.","Theriault C.","Tolstrup N.","Charlebois R.L.","Doolittle W.F.","Duguet M.","Gaasterland T.","Garrett R.A.","Ragan M.A.","Sensen C.W.","Van der Oost J."],"citationCrossReferences":[{"database":"PubMed","id":"11427726"},{"database":"DOI","id":"10.1073/pnas.141222098"}],"title":"The complete genome of the crenarchaeon Sulfolobus solfataricus P2.","publicationDate":"2001","journal":"Proc. 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