Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2001-03-01

AUTHORS

C Zubieta, X Z He, R A Dixon, J P Noel

ABSTRACT

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. More... »

PAGES

271-279

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/85029

DOI

http://dx.doi.org/10.1038/85029

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1014521492

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11224575


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