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http://purl.uniprot.org/citations/24361048http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24361048http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24361048http://www.w3.org/2000/01/rdf-schema#comment"The tripeptide chains of the ergopeptines, a class of pharmacologically important D-lysergic acid alkaloid peptides, are arranged in a unique bicyclic cyclol based on an amino-terminal α-hydroxyamino acid and a terminal orthostructure. D-lysergyl-tripeptides are assembled by the nonribosomal peptide synthetases LPS1 and LPS2 of the ergot fungus Claviceps purpurea and released as N-(D-lysergyl-aminoacyl)-lactams. We show total enzymatic synthesis of ergopeptines catalyzed by a Fe²⁺/2-ketoglutarate-dependent dioxygenase (EasH) in conjunction with LPS1/LPS2. Analysis of the reaction indicated that EasH introduces a hydroxyl group into N-(D-lysergyl-aminoacyl)-lactam at α-C of the aminoacyl residue followed by spontaneous condensation with the terminal lactam carbonyl group. Sequence analysis revealed that EasH belongs to the wide and diverse family of the phytanoyl coenzyme A hydroxylases. We provide a high-resolution crystal structure of EasH that is most similar to that of phytanoyl coenzyme A hydroxylase, PhyH, from human."xsd:string
http://purl.uniprot.org/citations/24361048http://purl.org/dc/terms/identifier"doi:10.1016/j.chembiol.2013.11.008"xsd:string
http://purl.uniprot.org/citations/24361048http://purl.org/dc/terms/identifier"doi:10.1016/j.chembiol.2013.11.008"xsd:string
http://purl.uniprot.org/citations/24361048http://purl.uniprot.org/core/author"Keller U."xsd:string
http://purl.uniprot.org/citations/24361048http://purl.uniprot.org/core/author"Keller U."xsd:string
http://purl.uniprot.org/citations/24361048http://purl.uniprot.org/core/author"Vogel D."xsd:string
http://purl.uniprot.org/citations/24361048http://purl.uniprot.org/core/author"Vogel D."xsd:string
http://purl.uniprot.org/citations/24361048http://purl.uniprot.org/core/author"Loll B."xsd:string
http://purl.uniprot.org/citations/24361048http://purl.uniprot.org/core/author"Loll B."xsd:string
http://purl.uniprot.org/citations/24361048http://purl.uniprot.org/core/author"Havemann J."xsd:string
http://purl.uniprot.org/citations/24361048http://purl.uniprot.org/core/author"Havemann J."xsd:string
http://purl.uniprot.org/citations/24361048http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24361048http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24361048http://purl.uniprot.org/core/name"Chem. Biol."xsd:string
http://purl.uniprot.org/citations/24361048http://purl.uniprot.org/core/name"Chem. Biol."xsd:string
http://purl.uniprot.org/citations/24361048http://purl.uniprot.org/core/pages"146-155"xsd:string
http://purl.uniprot.org/citations/24361048http://purl.uniprot.org/core/pages"146-155"xsd:string
http://purl.uniprot.org/citations/24361048http://purl.uniprot.org/core/title"Cyclolization of D-lysergic acid alkaloid peptides."xsd:string
http://purl.uniprot.org/citations/24361048http://purl.uniprot.org/core/title"Cyclolization of D-lysergic acid alkaloid peptides."xsd:string
http://purl.uniprot.org/citations/24361048http://purl.uniprot.org/core/volume"21"xsd:string
http://purl.uniprot.org/citations/24361048http://purl.uniprot.org/core/volume"21"xsd:string
http://purl.uniprot.org/citations/24361048http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24361048
http://purl.uniprot.org/citations/24361048http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24361048