Malonylation of Glucosylated N-Lauroylethanolamine: A New Pathway That Determines N-Acylethanolamine Metabolic Fate in Plants

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Article studying Malonylation of Glucosylated N-Lauroylethanolamine. Results indicate that glucosylation of NAE 12:0 by a yet to be determined glucosyltransferase and its subsequent malonylation by PMAT1 could represent a mechanism for modulating the biological activities of NAEs in plants.

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Khan, Bibi Rafeiza; Wherritt, Daniel J.; Huhman, David; Sumner, Lloyd W.; Chapman, Kent Dean & Blancaflor, Elison B. December 30, 2016.

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Article studying Malonylation of Glucosylated N-Lauroylethanolamine. Results indicate that glucosylation of NAE 12:0 by a yet to be determined glucosyltransferase and its subsequent malonylation by PMAT1 could represent a mechanism for modulating the biological activities of NAEs in plants.

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This research was originally published in the Journal of Biological Chemistry. Khan, Wherritt, Huhman, Sumner, Chapman, & Blancaflor. Malonylation of Glucosylated N-Lauroylethanolamine: A New Pathway That Determines N-Acylethanolamine Metabolic Fate in Plants. J. Biol. Chem. 2016; 291:27112-27121. © the American Society for Biochemistry and Molecular Biology

Abstract: N-Acylethanolamines (NAEs) are bioactive fatty acid derivatives present in trace amounts in many eukaryotes. Although NAEs have signaling and physiological roles in animals, little is known about their metabolic fate in plants. Our previous microarray analyses showed that inhibition of Arabidopsis thaliana seedling growth by exogenous N-lauroylethanolamine (NAE 12:0) was accompanied by the differential expression of multiple genes encoding small molecule-modifying enzymes. We focused on the gene At5g39050, which encodes a phenolic glucoside malonyltransferase 1 (PMAT1), to better understand the biological significance of NAE 12:0-induced gene expression changes. PMAT1 expression was induced 3–5-fold by exogenous NAE 12:0. PMAT1 knockouts (pmat1) had reduced sensitivity to the growth-inhibitory effects of NAE 12:0 compared with wild type leading to the hypothesis that PMAT1 might be a previously uncharacterized regulator of NAE metabolism in plants. To test this hypothesis, metabolic profiling of wild-type and pmat1 seedlings treated with NAE 12:0 was conducted. Wild-type seedlings treated with NAE 12:0 accumulated glucosylated and malonylated forms of this NAE species, and structures were confirmed using nuclear magnetic resonance (NMR) spectroscopy. By contrast, only the peak corresponding to NAE 12:0-glucoside was detected in pmat1. Recombinant PMAT1 catalyzed the reaction converting NAE 12:0-glucoside to NAE 12:0-mono- or -dimalonylglucosides providing direct evidence that this enzyme is involved in NAE 12:0-glucose malonylation. Taken together, our results indicate that glucosylation of NAE 12:0 by a yet to be determined glucosyltransferase and its subsequent malonylation by PMAT1 could represent a mechanism for modulating the biological activities of NAEs in plants.

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  • Journal of Biological Chemistry, 291(53), American Society for Biochemistry and Molecular Biology, December 30, 2016, pp. 1-10

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  • Publication Title: Journal of Biological Chemistry
  • Volume: 291
  • Issue: 53
  • Page Start: 27112
  • Page End: 27121
  • Peer Reviewed: Yes

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  • December 30, 2016

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Khan, Bibi Rafeiza; Wherritt, Daniel J.; Huhman, David; Sumner, Lloyd W.; Chapman, Kent Dean & Blancaflor, Elison B. Malonylation of Glucosylated N-Lauroylethanolamine: A New Pathway That Determines N-Acylethanolamine Metabolic Fate in Plants, article, December 30, 2016; [Rockville, Maryland]. (https://digital.library.unt.edu/ark:/67531/metadc1871084/: accessed April 25, 2025), University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu; crediting UNT College of Science.

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