Truncation of Medicago Truncatula Auxin Conjugate Hydrolases Alters Substrate Specificity
Document Type
Article
Publication Date
9-1-2011
Journal / Book Title
Plant Molecular Biology Reporter
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.
DOI
10.1007/s11105-010-0266-1
Montclair State University Digital Commons Citation
Campanella, James; Sigethy, Scott; and Ludwig-Müller, Jutta, "Truncation of Medicago Truncatula Auxin Conjugate Hydrolases Alters Substrate Specificity" (2011). Department of Biology Faculty Scholarship and Creative Works. 380.
https://digitalcommons.montclair.edu/biology-facpubs/380
Published Citation
Campanella, J.J., Sigethy, S. & Ludwig-Müller, J. Truncation of Medicago truncatula Auxin Conjugate Hydrolases Alters Substrate Specificity. Plant Mol Biol Rep 29, 745–752 (2011). https://doi.org/10.1007/s11105-010-0266-1
