Purification and properties of caffeic acid O-methyltransferase from alfalfa root nodules |
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| Authors: | Carroll P Vance Jeffrey W Bryan |
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| Institution: | U.S. Department of Agriculture, Science and Education Administration, Agriculture Research, Department of Agronomy and Plant Genetics, University of Minnesota, St. Paul, MN 55108, U.S.A. |
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| Abstract: | 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-hydroxyferulic acid. Chromatography on 1,6-diaminohexane agarose (AH-Sepharose-4B) linked with S-adenosyl-l-homocysteine (SAH) gave 35% recovery of enzyme activity. The Km values for caffeic acid and S-adenosyl-l-methionine were 58 and 4.1 μM, respectively. S-Adenosyl-l-homocysteine 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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| Keywords: | Leguminosae alfalfa nodules |
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