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http://purl.uniprot.org/citations/1396711http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1396711http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1396711http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/1396711http://www.w3.org/2000/01/rdf-schema#comment"A novel enzyme, arylalkyl acylamidase, which shows a strict specificity for N-acetyl arylalkylamines, but not acetanilide derivatives, was purified from the culture broth of Pseudomonas putida Sc2. The purified enzyme appeared to be homogeneous, as judged by native and SDS/PAGE. The enzyme has a molecular mass of approximately 150 kDa and consists of four identical subunits. The purified enzyme catalyzed the hydrolysis of N-acetyl-2-phenylethylamine to 2-phenylethylamine and acetic acid at the rate of 6.25 mumol.min-1.mg-1 at 30 degrees C. It also catalyzed the hydrolysis of various N-acetyl arylalkylamines containing a benzene or indole ring, and acetic acid arylalkyl esters. The enzyme did not hydrolyze acetanilide, N-acetyl aliphatic amines, N-acetyl amino acids, N-acetyl amino sugars or acylthiocholine. The apparent Km for N-acetylbenzylamine, N-acetyl-2-phenylethylamine and N-acetyl-3-phenylpropylamine are 41 mM, 0.31 mM and 1.6 mM, respectively. The purified enzyme was sensitive to thiol reagents such as Ag2SO4, HgCl2 and p-chloromercuribenzoic acid, and its activity was enhanced by divalent metal ions such as Zn2+, Mg2+ and Mn2+."xsd:string
http://purl.uniprot.org/citations/1396711http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1992.tb17299.x"xsd:string
http://purl.uniprot.org/citations/1396711http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1992.tb17299.x"xsd:string
http://purl.uniprot.org/citations/1396711http://purl.uniprot.org/core/author"Shimizu S."xsd:string
http://purl.uniprot.org/citations/1396711http://purl.uniprot.org/core/author"Shimizu S."xsd:string
http://purl.uniprot.org/citations/1396711http://purl.uniprot.org/core/author"Yamada H."xsd:string
http://purl.uniprot.org/citations/1396711http://purl.uniprot.org/core/author"Yamada H."xsd:string
http://purl.uniprot.org/citations/1396711http://purl.uniprot.org/core/author"Ogawa J."xsd:string
http://purl.uniprot.org/citations/1396711http://purl.uniprot.org/core/author"Ogawa J."xsd:string
http://purl.uniprot.org/citations/1396711http://purl.uniprot.org/core/author"Chung M.C.-M."xsd:string
http://purl.uniprot.org/citations/1396711http://purl.uniprot.org/core/author"Chung M.C.-M."xsd:string
http://purl.uniprot.org/citations/1396711http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1396711http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1396711http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/1396711http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/1396711http://purl.uniprot.org/core/pages"375-382"xsd:string
http://purl.uniprot.org/citations/1396711http://purl.uniprot.org/core/pages"375-382"xsd:string
http://purl.uniprot.org/citations/1396711http://purl.uniprot.org/core/title"Purification and characterization of a novel enzyme, arylalkyl acylamidase, from Pseudomonas putida Sc2."xsd:string
http://purl.uniprot.org/citations/1396711http://purl.uniprot.org/core/title"Purification and characterization of a novel enzyme, arylalkyl acylamidase, from Pseudomonas putida Sc2."xsd:string
http://purl.uniprot.org/citations/1396711http://purl.uniprot.org/core/volume"209"xsd:string
http://purl.uniprot.org/citations/1396711http://purl.uniprot.org/core/volume"209"xsd:string
http://purl.uniprot.org/citations/1396711http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1396711