Glucose ester enabled acylation in plant specialized metabolism

Alexander E. Wilson, Hosea D. Matel, Li Tian

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


Acylation of core compound skeletons, together with other modifications, plays a significant role in producing the incredible diversity of plant specialized metabolites. Two major classes of acyltransferases, the BAHD and serine carboxypeptidase-like (SCPL) acyltransferases, can bring together through acylation compounds from the same or divergent metabolic pathways. BAHD acyltransferases (BAHD-ATs) employ CoA thioesters as the activated substrate, SCPL acyltransferases (SCPL-ATs), on the other hand, utilize β-acetal esters, typically glucose esters formed by UDP glycosyltransferases (UGTs). While the general trend of high energy glucose ester enabled acyltransfers is seen throughout the spermatophytes (seed plants), the specific metabolites that are conjugated appear to be lineage specific. In this review, we examine the reaction mechanism, biochemical property and evolutionary relationship of SCPL-ATs that utilize various glucose ester donors and acceptors from the same or different plant specialized metabolic pathways. The occurrence and taxonomic distribution of galloylated flavan-3-ols, hydrolyzable tannins and galloylated flavonols are also evaluated. Furthermore, glucose ester (acyl donor)-forming UGT activities and the subcellular localization of the UGT and SCPL-AT catalyzed reactions are discussed.

Original languageEnglish (US)
Pages (from-to)1-18
Number of pages18
JournalPhytochemistry Reviews
StateAccepted/In press - Apr 26 2016


  • Acyltransferase
  • BAHD
  • Glucose ester
  • Serinecarboxypeptidase like
  • UDP glycosyltransferase

ASJC Scopus subject areas

  • Plant Science
  • Biotechnology


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