Functional Characterization of an Anthocyanin Dimalonyltransferase in Maize

Michael Paulsmeyer, John Juvik

Research output: Contribution to journalArticlepeer-review

Abstract

Anthocyanins are pigments with appealing hues that are currently being used as sources of natural colorants. The interaction of acylation on the stability of anthocyanin molecules has long been known. Maize is an abundant source of malonylglucoside and dimalonylglucoside anthocyanins. The enzyme Aat1 is an anthocyanin acyltransferase known to synthesize the majority of acylated anthocyanins in maize. In this paper, we characterize the substrate specificity and reaction kinetics of Aat1. It was found that Aat1 has anthocyanin 3-O-glucoside dimalonyltransferase activity and is only the second enzyme of this type characterized to this date. Our results indicate that Aat1 can utilize malonyl-CoA; succinyl-CoA and every anthocyanin 3-O-glucoside tested. Results of this study provide insight into the structure–function relations of dimalonyltransferases and give a unique insight into the activity of monocot anthocyanin acyltransferases.
Original languageEnglish (US)
JournalMolecules
Volume26
Issue number7
DOIs
StatePublished - Apr 2021

Keywords

  • acyltransferase
  • malonyltransferase
  • enzyme kinetics
  • cyanidin
  • acylation

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