Truncation of Medicago truncatula Auxin Conjugate Hydrolases Alters Substrate Specificity

James Campanella, Scott Sigethy, Jutta Ludwig-Müller

Research output: Contribution to journalArticleResearchpeer-review

8 Citations (Scopus)

Abstract

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
Volume29
Issue number3
DOIs
StatePublished - 1 Sep 2011

Fingerprint

Medicago truncatula
Indoleacetic Acids
Hydrolases
substrate specificity
Substrate Specificity
hydrolases
auxins
Methionine
methionine
Fabaceae
legumes
Clone Cells
Head
clones
Amino Acids
amino acids
Enzymes
enzymes
Proteins
proteins

Keywords

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

Cite this

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Truncation of Medicago truncatula Auxin Conjugate Hydrolases Alters Substrate Specificity. / Campanella, James; Sigethy, Scott; Ludwig-Müller, Jutta.

In: Plant Molecular Biology Reporter, Vol. 29, No. 3, 01.09.2011, p. 745-752.

Research output: Contribution to journalArticleResearchpeer-review

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