Structure-function relationships of wheat flavone O-methyltransferase: Homology modeling and site-directed mutagenesis.

ABSTRACT:

Background

Wheat (Triticum aestivum L.) O-methyltransferase (TaOMT2) catalyzes the sequential methylation of the flavone, tricetin, to its 3'-methyl- (selgin), 3',5'-dimethyl- (tricin) and 3',4',5'-trimethyl ether derivatives. Tricin, a potential multifunctional nutraceutical, is the major enzyme reaction product. These successive methylations raised the question as to whether they take place in one, or different active sites. We constructed a 3-D model of this protein using the crystal structure of the highly homologous Medicago sativa caffeic acid/5-hydroxyferulic acid O-methyltransferase (MsCOMT) as a template with the aim of proposing a mechanism for multiple methyl transfer reactions in wheat.

Results

This model revealed unique structural features of TaOMT2 which permit

SUBMITTER: Zhou JM 

PROVIDER: S-EPMC3017781 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature