http://purl.uniprot.org/citations/10610793 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/10610793 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/10610793 | http://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/10610793 | http://purl.org/dc/terms/identifier | "doi:10.1006/jmbi.1999.3255"xsd:string |
http://purl.uniprot.org/citations/10610793 | http://purl.org/dc/terms/identifier | "doi:10.1006/jmbi.1999.3255"xsd:string |
http://purl.uniprot.org/citations/10610793 | http://purl.uniprot.org/core/author | "Capitani G."xsd:string |
http://purl.uniprot.org/citations/10610793 | http://purl.uniprot.org/core/author | "Capitani G."xsd:string |
http://purl.uniprot.org/citations/10610793 | http://purl.uniprot.org/core/author | "Feng L."xsd:string |
http://purl.uniprot.org/citations/10610793 | http://purl.uniprot.org/core/author | "Feng L."xsd:string |
http://purl.uniprot.org/citations/10610793 | http://purl.uniprot.org/core/author | "Hohenester E."xsd:string |
http://purl.uniprot.org/citations/10610793 | http://purl.uniprot.org/core/author | "Hohenester E."xsd:string |
http://purl.uniprot.org/citations/10610793 | http://purl.uniprot.org/core/author | "Jansonius J.N."xsd:string |
http://purl.uniprot.org/citations/10610793 | http://purl.uniprot.org/core/author | "Jansonius J.N."xsd:string |
http://purl.uniprot.org/citations/10610793 | http://purl.uniprot.org/core/author | "Kirsch J.F."xsd:string |
http://purl.uniprot.org/citations/10610793 | http://purl.uniprot.org/core/author | "Kirsch J.F."xsd:string |
http://purl.uniprot.org/citations/10610793 | http://purl.uniprot.org/core/author | "Storici P."xsd:string |
http://purl.uniprot.org/citations/10610793 | http://purl.uniprot.org/core/author | "Storici P."xsd:string |
http://purl.uniprot.org/citations/10610793 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
http://purl.uniprot.org/citations/10610793 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
http://purl.uniprot.org/citations/10610793 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
http://purl.uniprot.org/citations/10610793 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
http://purl.uniprot.org/citations/10610793 | http://purl.uniprot.org/core/pages | "745-756"xsd:string |
http://purl.uniprot.org/citations/10610793 | http://purl.uniprot.org/core/pages | "745-756"xsd:string |
http://purl.uniprot.org/citations/10610793 | http://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/10610793 | http://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 |