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http://purl.uniprot.org/citations/11248691http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11248691http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11248691http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/11248691http://www.w3.org/2000/01/rdf-schema#comment"Cyclic dipeptide oxidase is a novel enzyme that specifically catalyzes the formation of alpha,beta-dehydro-Phe (Delta Phe) and alpha,beta-dehydro-Leu (Delta Leu) residues during the biosynthesis of albonoursin, cyclo(Delta Phe-Delta Leu), an antibiotic produced by Streptomyces noursei. It was purified 600-fold with a 30% overall recovery, and consists of the association of a single type of subunit with a relative molecular mass of 21,066 resulting in a large homopolymer of relative molecular mass over 2,000,000. The enzyme exhibits a typical flavoprotein spectrum with maxima at 343.5 and 447.5 nm, the flavin prosthetic group being covalently bound to the protein. The catalytic reaction of the natural substrate cyclo(L-Phe-L-Leu) occurs in a two-step sequential reaction leading first to cyclo(alpha,beta-dehydro-Phe-L-Leu) and finally to albonoursin. Kinetic parameters for the first step were determined (K(m) = 53 microM; k = 0.69 s(-1)). The enzyme was shown to catalyze the conversion of a variety of cyclo(dipeptides) and can be reoxidized at the expense of molecular oxygen by producing H(2)O(2). This reaction mechanism, which differs from those already described for the formation of alpha,beta-dehydro-amino acids, might consist of the transient formation of an intermediate imine followed by its rearrangement into an alpha,beta-dehydro-residue."xsd:string
http://purl.uniprot.org/citations/11248691http://purl.org/dc/terms/identifier"doi:10.1046/j.1432-1033.2001.02038.x"xsd:string
http://purl.uniprot.org/citations/11248691http://purl.org/dc/terms/identifier"doi:10.1046/j.1432-1033.2001.02038.x"xsd:string
http://purl.uniprot.org/citations/11248691http://purl.uniprot.org/core/author"Menez A."xsd:string
http://purl.uniprot.org/citations/11248691http://purl.uniprot.org/core/author"Menez A."xsd:string
http://purl.uniprot.org/citations/11248691http://purl.uniprot.org/core/author"Fusai G."xsd:string
http://purl.uniprot.org/citations/11248691http://purl.uniprot.org/core/author"Fusai G."xsd:string
http://purl.uniprot.org/citations/11248691http://purl.uniprot.org/core/author"Genet R."xsd:string
http://purl.uniprot.org/citations/11248691http://purl.uniprot.org/core/author"Genet R."xsd:string
http://purl.uniprot.org/citations/11248691http://purl.uniprot.org/core/author"Gondry M."xsd:string
http://purl.uniprot.org/citations/11248691http://purl.uniprot.org/core/author"Gondry M."xsd:string
http://purl.uniprot.org/citations/11248691http://purl.uniprot.org/core/author"Lautru S."xsd:string
http://purl.uniprot.org/citations/11248691http://purl.uniprot.org/core/author"Lautru S."xsd:string
http://purl.uniprot.org/citations/11248691http://purl.uniprot.org/core/author"Meunier G."xsd:string
http://purl.uniprot.org/citations/11248691http://purl.uniprot.org/core/author"Meunier G."xsd:string
http://purl.uniprot.org/citations/11248691http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11248691http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11248691http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/11248691http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/11248691http://purl.uniprot.org/core/pages"1712-1721"xsd:string
http://purl.uniprot.org/citations/11248691http://purl.uniprot.org/core/pages"1712-1721"xsd:string
http://purl.uniprot.org/citations/11248691http://purl.uniprot.org/core/title"Cyclic dipeptide oxidase from Streptomyces noursei. Isolation, purification and partial characterization of a novel, amino acyl alpha,beta-dehydrogenase."xsd:string