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

Sanchez Parra, Beatriz; Frerigmann, Henning; Perez Alonso, Marta Marina; Carrasco Loba, Víctor; Jost, Ricarda; Hentrich, Mathias y 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.

Descripción

Título: Characterization of four bifunctional plant IAM/PAM-amidohydrolases capable of contributing to auxin biosynthesis.
Autor/es:
  • Sanchez Parra, Beatriz
  • Frerigmann, Henning
  • Perez Alonso, Marta Marina
  • Carrasco Loba, Víctor
  • Jost, Ricarda
  • Hentrich, Mathias
  • Pollmann, Stephan
Tipo de Documento: Artículo
Título de Revista/Publicación: Plants
Fecha: Agosto 2014
Volumen: 3
Materias:
Escuela: Centro de Investigación en Biotecnología y Genómica de Plantas (CBGP) (UPM)
Departamento: Biotecnologia [hasta 2014]
Licencias Creative Commons: Reconocimiento - Sin obra derivada - No comercial

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Resumen

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.

Más información

ID de Registro: 30778
Identificador DC: http://oa.upm.es/30778/
Identificador OAI: oai:oa.upm.es:30778
Identificador DOI: 10.3390/plants3030324
URL Oficial: http://www.mdpi.com/2223-7747/3/3/324
Depositado por: Memoria Investigacion
Depositado el: 02 Dic 2014 17:57
Ultima Modificación: 02 Dic 2014 17:57
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