RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/10610793http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10610793http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10610793http://www.w3.org/2000/01/rdf-schema#comment"The 2.4 A crystal structure of the vitamin B6-dependent enzyme 1-aminocyclopropane-1-carboxylate (ACC) synthase is described. This enzyme catalyses the committed step in the biosynthesis of ethylene, a plant hormone that is responsible for the initiation of fruit ripening and for regulating many other developmental processes. ACC synthase has 15 % sequence identity with the well-studied aspartate aminotransferase, and a completely different catalytic activity yet the overall folds and the active sites are very similar. The new structure together with available biochemical data enables a comparative mechanistic analysis that largely explains the catalytic roles of the conserved and non-conserved active site residues. An external aldimine reaction intermediate (external aldimine with ACC, i.e. with the product) has been modeled. The new structure provides a basis for the rational design of inhibitors with broad agricultural applications."xsd:string
http://purl.uniprot.org/citations/10610793http://purl.org/dc/terms/identifier"doi:10.1006/jmbi.1999.3255"xsd:string
http://purl.uniprot.org/citations/10610793http://purl.org/dc/terms/identifier"doi:10.1006/jmbi.1999.3255"xsd:string
http://purl.uniprot.org/citations/10610793http://purl.uniprot.org/core/author"Capitani G."xsd:string
http://purl.uniprot.org/citations/10610793http://purl.uniprot.org/core/author"Capitani G."xsd:string
http://purl.uniprot.org/citations/10610793http://purl.uniprot.org/core/author"Feng L."xsd:string
http://purl.uniprot.org/citations/10610793http://purl.uniprot.org/core/author"Feng L."xsd:string
http://purl.uniprot.org/citations/10610793http://purl.uniprot.org/core/author"Hohenester E."xsd:string
http://purl.uniprot.org/citations/10610793http://purl.uniprot.org/core/author"Hohenester E."xsd:string
http://purl.uniprot.org/citations/10610793http://purl.uniprot.org/core/author"Jansonius J.N."xsd:string
http://purl.uniprot.org/citations/10610793http://purl.uniprot.org/core/author"Jansonius J.N."xsd:string
http://purl.uniprot.org/citations/10610793http://purl.uniprot.org/core/author"Kirsch J.F."xsd:string
http://purl.uniprot.org/citations/10610793http://purl.uniprot.org/core/author"Kirsch J.F."xsd:string
http://purl.uniprot.org/citations/10610793http://purl.uniprot.org/core/author"Storici P."xsd:string
http://purl.uniprot.org/citations/10610793http://purl.uniprot.org/core/author"Storici P."xsd:string
http://purl.uniprot.org/citations/10610793http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10610793http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10610793http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/10610793http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/10610793http://purl.uniprot.org/core/pages"745-756"xsd:string
http://purl.uniprot.org/citations/10610793http://purl.uniprot.org/core/pages"745-756"xsd:string
http://purl.uniprot.org/citations/10610793http://purl.uniprot.org/core/title"Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene."xsd:string
http://purl.uniprot.org/citations/10610793http://purl.uniprot.org/core/title"Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene."xsd:string