Phytochemistry p. 41 - 44 (1981)
Update date:2022-08-11
Topics:
Vance, Carroll P.
Bryan, Jeffrey W.
An O-methyltransferase which catalyses the methylation of caffeic acid to ferulic acid using S-adenosyl-L-methionine as methyl donor has been isolated and purified ca. 70-fold from root nodules of alfalfa.The enzyme also catalysed the methylation of 5-fydroxyferulic acid.Chromatography on 1,6-diaminohexane agarose (AH-Sepharose4B) linked with S-adenosyl-L-homocysteine (SAH) gave 35 percent recovery of enzyme activity.The Km values for caffeic acid ans S-adenosyl-L-methionine were 58 and 4.1 μM, respectively.S-Adenosyl-L-homocysteins was a potent competitive inhibitor of S-adenosyl-L-methionine with a Ki of 0.44 μM.The MW of the enzyme was ca. 103 000 determined by gel filtration chromatography.
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