Evidence for the formation of methoxyl groups of ferulic and sinapic acids in Bambusa by the same O-methyltransferase

Abstract

The two methylation reactions, i.e. caffeate to ferulate (FA) and 5-hydroxyferulate to sinapate (SA), in the biosynthesis of guaiacyl and syringyl lignins in angiosperms were demonstrated to be catalyzed by the same enzyme in bamboo. This follows from the facts that: the ratio (SA/FA) obtained for O-methyltransferase remains constant during purification of the enzyme; chromatography on DEAE-cellulose, Sephadex G100 and G200, and analyses by polyacrylamide gel electrophoresis and isoelectric focusing in pH gradients showed that the two methylating activities belonged to a single enzyme protein; caffeate and 5-hydroxyferulate compete each other in the formation of the enzyme-substrate complex, the latter substrate showing greater affinity for the enzyme. Thus, feedback control may operate at the methylation step, caffeate to FA, in biosynthesis of angiosperm lignin.