Characterization of four bifunctional plant IAM/PAM-amidohydrolases capable of contributing to auxin biosynthesis.

Sanchez Parra, Beatriz and Frerigmann, Henning and Perez Alonso, Marta Marina and Carrasco Loba, Víctor and Jost, Ricarda and Hentrich, Mathias and Pollmann, Stephan (2014). Characterization of four bifunctional plant IAM/PAM-amidohydrolases capable of contributing to auxin biosynthesis.. "Plants", v. 3 (n. 3); pp. 327-347. ISSN 2223-7747. https://doi.org/10.3390/plants3030324.

Description

Title: Characterization of four bifunctional plant IAM/PAM-amidohydrolases capable of contributing to auxin biosynthesis.
Author/s:
  • Sanchez Parra, Beatriz
  • Frerigmann, Henning
  • Perez Alonso, Marta Marina
  • Carrasco Loba, Víctor
  • Jost, Ricarda
  • Hentrich, Mathias
  • Pollmann, Stephan
Item Type: Article
Título de Revista/Publicación: Plants
Date: August 2014
ISSN: 2223-7747
Volume: 3
Subjects:
Faculty: Centro de Investigación en Biotecnología y Genómica de Plantas (CBGP) (UPM)
Department: Biotecnologia [hasta 2014]
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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Abstract

Amidases [EC 3.5.1.4] capable of converting indole-3-acetamide (IAM) into the major plant growth hormone indole-3-acetic acid (IAA) are assumed to be involved in auxin de novo biosynthesis. With the emerging amount of genomics data, it was possible to identify over forty proteins with substantial homology to the already characterized amidases from Arabidopsis and tobacco. The observed high conservation of amidase-like proteins throughout the plant kingdom may suggest an important role of theses enzymes in plant development. Here, we report cloning and functional analysis of four, thus far, uncharacterized plant amidases from Oryza sativa, Sorghum bicolor, Medicago truncatula, and Populus trichocarpa. Intriguingly, we were able to demonstrate that the examined amidases are also capable of converting phenyl-2-acetamide (PAM) into phenyl-2-acetic acid (PAA), an auxin endogenous to several plant species including Arabidopsis. Furthermore, we compared the subcellular localization of the enzymes to that of Arabidopsis AMI1, providing further evidence for similar enzymatic functions. Our results point to the presence of a presumably conserved pathway of auxin biosynthesis via IAM, as amidases, both of monocot, and dicot origins, were analyzed.

Funding Projects

TypeCodeAcronymLeaderTitle
Government of SpainBFU2011-25925SYSBIOAUXUNIVERSIDAD POLITECNICA DE MADRIDA Systems Biology approach to disclose auxin synthesis in plants
FP7303744UnspecifiedUnspecifiedUnspecified

More information

Item ID: 30778
DC Identifier: http://oa.upm.es/30778/
OAI Identifier: oai:oa.upm.es:30778
DOI: 10.3390/plants3030324
Official URL: http://www.mdpi.com/2223-7747/3/3/324
Deposited by: Memoria Investigacion
Deposited on: 02 Dec 2014 17:57
Last Modified: 11 Apr 2019 12:02
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