N-malonyltransferases from peanut

Arch Biochem Biophys. 1984 Nov 15;235(1):218-27. doi: 10.1016/0003-9861(84)90271-6.


Three distinct N-malonyltransferases were purified from peanut seedlings, accepting either anthranilic acid, D-tryptophan, or 3,4-dichloroaniline, respectively, as a substrate. Partially purified malonyl-CoA:D-tryptophan malonyltransferase also catalyzed the formation of the corresponding malonic acid conjugate when 1-aminocyclopropane-1-carboxylic acid was employed as a substrate. These N-malonyltransferases were clearly distinguished from several O-malonyltransferase activities also present in the same seedlings. N-Malonic acid conjugates have been previously isolated from peanut either as a natural constituent or after feeding with xenobiotics. By analogy to the results reported with cultured parsley cells, multiple malonyltransferases in peanut may have a role in vacuolar transport. Crude extracts of young peanut seedlings were incapable of hydrolyzing the respective N-malonic acid conjugates. However, dialyzed extracts of older plants released malonic acid from malonyl-1-aminocyclopropane-1-carboxylic acid but not from malonyl-3,4-dichloroaniline, suggesting that some N-malonic acid conjugates may be metabolized in plants which are approaching senescence.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyltransferases / isolation & purification*
  • Arachis / enzymology
  • Isoenzymes / isolation & purification
  • Kinetics
  • Malonates / metabolism
  • Plants / enzymology*
  • Substrate Specificity


  • Isoenzymes
  • Malonates
  • malonic acid
  • Acyltransferases
  • malonyl-CoA-3,4-dichloroaniline N-malonyltransferase
  • malonyl-CoA-D-tryptophan N-malonyltransferase
  • malonyl-CoA-anthranilic acid N-malonyltransferase