PMID: 2499260Jun 1, 1989Paper

S-adenosyl-L-methionine:trans-caffeoyl-coenzyme A 3-O-methyltransferase from elicitor-treated parsley cell suspension cultures

Archives of Biochemistry and Biophysics
A E PakuschU Matern

Abstract

An S-adenosyl-L-methionine:caffeoyl-CoA 3-O-methyltransferase was purified 82-fold from elicitor-induced parsley cell suspension cultures by ammonium sulfate fractionation, anionic exchange and hydrophobic interaction chromatographies, and chromatofocusing. The enzyme has an apparent pI of 5.7 and a molecular weight of approx 48,000 determined by gel filtration chromatography. Maximal activity was observed at pH 7.5 in 50 mM phosphate or Tris-HCl buffers and the additional presence of 0.5 M NaCl. The methyltransferase activity was dependent on Mg2+, whereas EDTA, Mn2+, and Ca2+ inhibited the reaction. The partially purified enzyme efficiently catalyzed the methylation of caffeoyl-CoA, but also accepted with low affinity various other caffeic esters as substrates. Dark-grown parsley cells contained considerable methyltransferase activity which was nevertheless increased approx threefold within 12 h following the addition of a crude fungal elicitor to the cell suspensions. We propose that the O-methyltransferase activity is an important component in the rapid resistance response of the cells, which depends on the formation of cell wall-bound ferulic polymers.

References

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Citations

Jun 30, 2001·Phytochemistry·Z H YeD S Himmelsbach
Aug 29, 2003·Phytochemistry·Kerstin Kranz, Maike Petersen
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Nov 15, 2017·BMC Genomics·Weiying ZengXiangmin Tang
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Apr 10, 2010·Journal of Integrative Plant Biology·Anna Kärkönen, Sanna Koutaniemi
Oct 31, 2009·The Journal of Biological Chemistry·Mohammad-Wadud Bhuiya, Chang-Jun Liu

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