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http://purl.uniprot.org/citations/28092359http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28092359http://www.w3.org/2000/01/rdf-schema#comment"Substrate channeling has emerged as a common mechanism for enzymatic intermediate transfer. A conspicuous gap in knowledge concerns the use of covalent lysine imines in the transfer of carbonyl-group-containing intermediates, despite their wideuse in enzymatic catalysis. Here we show how imine chemistry operates in the transfer of covalent intermediates in pyridoxal 5'-phosphate biosynthesis by the Arabidopsis thaliana enzyme Pdx1. An initial ribose 5-phosphate lysine imine is converted to the chromophoric I320 intermediate, simultaneously bound to two lysine residues and partially vacating the active site, which creates space for glyceraldehyde 3-phosphate to bind. Crystal structures show how substrate binding, catalysis and shuttling are coupled to conformational changes around strand β6 of the Pdx1 (βα)8-barrel. The dual-specificity active site and imine relay mechanism for migration of carbonyl intermediates provide elegant solutions to the challenge of coordinating a complex sequence of reactions that follow a path of over 20 Å between substrate- and product-binding sites."xsd:string
http://purl.uniprot.org/citations/28092359http://purl.org/dc/terms/identifier"doi:10.1038/nchembio.2273"xsd:string
http://purl.uniprot.org/citations/28092359http://purl.uniprot.org/core/author"Begley T.P."xsd:string
http://purl.uniprot.org/citations/28092359http://purl.uniprot.org/core/author"Ealick S.E."xsd:string
http://purl.uniprot.org/citations/28092359http://purl.uniprot.org/core/author"Royant A."xsd:string
http://purl.uniprot.org/citations/28092359http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/28092359http://purl.uniprot.org/core/author"Sinning I."xsd:string
http://purl.uniprot.org/citations/28092359http://purl.uniprot.org/core/author"Guedez G."xsd:string
http://purl.uniprot.org/citations/28092359http://purl.uniprot.org/core/author"Tews I."xsd:string
http://purl.uniprot.org/citations/28092359http://purl.uniprot.org/core/author"Windeisen V."xsd:string
http://purl.uniprot.org/citations/28092359http://purl.uniprot.org/core/author"Weber S."xsd:string
http://purl.uniprot.org/citations/28092359http://purl.uniprot.org/core/author"Evans G."xsd:string
http://purl.uniprot.org/citations/28092359http://purl.uniprot.org/core/author"Strohmeier M."xsd:string
http://purl.uniprot.org/citations/28092359http://purl.uniprot.org/core/author"Hanes J.W."xsd:string
http://purl.uniprot.org/citations/28092359http://purl.uniprot.org/core/author"Rodrigues M.J."xsd:string
http://purl.uniprot.org/citations/28092359http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28092359http://purl.uniprot.org/core/name"Nat Chem Biol"xsd:string
http://purl.uniprot.org/citations/28092359http://purl.uniprot.org/core/pages"290-294"xsd:string
http://purl.uniprot.org/citations/28092359http://purl.uniprot.org/core/title"Lysine relay mechanism coordinates intermediate transfer in vitamin B6 biosynthesis."xsd:string
http://purl.uniprot.org/citations/28092359http://purl.uniprot.org/core/volume"13"xsd:string
http://purl.uniprot.org/citations/28092359http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28092359
http://purl.uniprot.org/citations/28092359http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/28092359
http://purl.uniprot.org/uniprot/#_F6M3L4-mappedCitation-28092359http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28092359
http://purl.uniprot.org/uniprot/#_O80448-mappedCitation-28092359http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28092359