| http://purl.uniprot.org/citations/11224575 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11224575 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11224575 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/11224575 | http://www.w3.org/2000/01/rdf-schema#comment | "Chalcone O-methyltransferase (ChOMT) and isoflavone O-methyltransferase (IOMT) are S-adenosyl-l-methionine (SAM) dependent plant natural product methyltransferases involved in secondary metabolism in Medicago sativa (alfalfa). Here we report the crystal structure of ChOMT in complex with the product S-adenosyl-l-homocysteine and the substrate isoliquiritigenin (4,2',4'-trihydroxychalcone) refined to 1.8 A as well as the crystal structure of IOMT in complex with the products S-adenosyl-l-homocysteine and isoformononetin (4'-hydroxy-7-methoxyisoflavone) refined to 1.4 A. These two OMTs constitute the first plant methyltransferases to be structurally characterized and reveal a novel oligomerization domain and the molecular determinants for substrate selection. As such, this work provides a structural basis for understanding the substrate specificity of the diverse family of plant OMTs and facilitates the engineering of novel activities in this extensive class of natural product biosynthetic enzymes."xsd:string |
| http://purl.uniprot.org/citations/11224575 | http://purl.org/dc/terms/identifier | "doi:10.1038/85029"xsd:string |
| http://purl.uniprot.org/citations/11224575 | http://purl.org/dc/terms/identifier | "doi:10.1038/85029"xsd:string |
| http://purl.uniprot.org/citations/11224575 | http://purl.uniprot.org/core/author | "Dixon R.A."xsd:string |
| http://purl.uniprot.org/citations/11224575 | http://purl.uniprot.org/core/author | "Dixon R.A."xsd:string |
| http://purl.uniprot.org/citations/11224575 | http://purl.uniprot.org/core/author | "He X.-Z."xsd:string |
| http://purl.uniprot.org/citations/11224575 | http://purl.uniprot.org/core/author | "He X.-Z."xsd:string |
| http://purl.uniprot.org/citations/11224575 | http://purl.uniprot.org/core/author | "Noel J.P."xsd:string |
| http://purl.uniprot.org/citations/11224575 | http://purl.uniprot.org/core/author | "Noel J.P."xsd:string |
| http://purl.uniprot.org/citations/11224575 | http://purl.uniprot.org/core/author | "Zubieta C."xsd:string |
| http://purl.uniprot.org/citations/11224575 | http://purl.uniprot.org/core/author | "Zubieta C."xsd:string |
| http://purl.uniprot.org/citations/11224575 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11224575 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11224575 | http://purl.uniprot.org/core/name | "Nat. Struct. Biol."xsd:string |
| http://purl.uniprot.org/citations/11224575 | http://purl.uniprot.org/core/name | "Nat. Struct. Biol."xsd:string |
| http://purl.uniprot.org/citations/11224575 | http://purl.uniprot.org/core/pages | "271-279"xsd:string |
| http://purl.uniprot.org/citations/11224575 | http://purl.uniprot.org/core/pages | "271-279"xsd:string |
| http://purl.uniprot.org/citations/11224575 | http://purl.uniprot.org/core/title | "Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases."xsd:string |
| http://purl.uniprot.org/citations/11224575 | http://purl.uniprot.org/core/title | "Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases."xsd:string |
| http://purl.uniprot.org/citations/11224575 | http://purl.uniprot.org/core/volume | "8"xsd:string |
| http://purl.uniprot.org/citations/11224575 | http://purl.uniprot.org/core/volume | "8"xsd:string |
| http://purl.uniprot.org/citations/11224575 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11224575 |