Truncation of Medicago truncatula Auxin Conjugate Hydrolases Alters Substrate Specificity

James J. Campanella, Scott Sigethy, Jutta Ludwig-Müller

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11 Scopus citations


We have previously isolated and characterized a family of auxin amino acid conjugate hydrolases from the legume Medicago truncatula. All characterized members of this family possess a conserved second methionine within the predicted hydrolase domain. We therefore constructed 5′-truncated clones of the hydrolases to investigate whether this methionine could have a potential function. Overall, the hydrolases exhibited altered substrate specificities towards a variety of auxin conjugates tested, with a somewhat broadened substrate range. In vitro hydrolase activity increased over wild-type in several of the shortened proteins, but only for some substrates. The 5′ "head" domain may be serving a regulatory function in the full-length versions of the enzymes or could provide a mechanism to broaden the substrate range in vivo.

Original languageEnglish
Pages (from-to)745-752
Number of pages8
JournalPlant Molecular Biology Reporter
Issue number3
StatePublished - Sep 2011


  • Auxin conjugate hydrolase
  • Enzyme activity
  • Enzyme regulation
  • Indole-3-acetic acid
  • Indole-3-butyric acid
  • Medicago truncatula


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