Unser 10. Leibniz Plant Biochemistry Symposium am 7. und 8. Mai war ein großer Erfolg. Thematisch ging es in diesem Jahr um neue Methoden und Forschungsansätze der Naturstoffchemie. Die exzellenten Vorträge über Wirkstoffe…
Omanische Heilpflanze im Fokus der Phytochemie IPB-Wissenschaftler und Partner aus Dhofar haben jüngst die omanische Heilpflanze Terminalia dhofarica unter die phytochemische Lupe genommen. Die Pflanze ist reich an…
Geschmack ist vorhersagbar: Mit FlavorMiner. FlavorMiner heißt das Tool, das IPB-Chemiker und Partner aus Kolumbien jüngst entwickelt haben. Das Programm kann, basierend auf maschinellem Lernen (KI), anhand der…
Lukačin, R.; Matern, U.; Hehmann, M.; Specker, S.; Vogt, T.;Corrigendum to “Cations modulate the substrate specificity of bifunctional class I O-methyltransferase from Ammi majus” [FEBS Lett. 577 (2004) 367-370]FEBS Lett.583855-855(2009)DOI: 10.1016/j.febslet.2009.01.050
Lukačin, R.; Matern, U.; Specker, S.; Vogt, T.;Cations modulate the substrate specificity of bifunctional class I O-methyltransferase from Ammi majusFEBS Lett.577367-370(2004)DOI: 10.1016/j.febslet.2004.10.032
Caffeoyl‐coenzyme A O‐methyltransferase cDNA was cloned from dark‐grown Ammi majus L. (Apiaceae) cells treated with a crude fungal elicitor and the open reading frame was expressed in Escherichia coli . The translated polypeptide of 27.1‐kDa shared significant identity to other members of this highly conserved class of proteins and was 98.8% identical to the corresponding O‐methyltransferase from parsley. For biochemical characterization, the recombinant enzyme could be purified to apparent homogeneity by metal‐affinity chromatography, although the recombinant enzyme did not contain any affinity tag. Based on sequence analysis and substrate specificity, the enzyme classifies as a cation‐dependent O‐methyltransferase with pronounced preference for caffeoyl coenzyme A, when assayed in the presence of Mg2+‐ions. Surprisingly, however, the substrate specificity changed dramatically, when Mg2+ was replaced by Mn2+ or Co2+ in the assays. This effect could point to yet unknown functions and substrate specificities in situ and suggests promiscuous roles for the lignin specific cluster of plant O‐methyltransferases.