INSTITUTO TECNOLOGICO DE CHASCOMUS
Unidad Ejecutora - UE
congresos y reuniones científicas
DEFINING NOVEL PLANT POLYAMINE OXIDASE SUBFAMILIES THROUGH MOLECULAR MODELING AND SEQUENCE ANALYSIS
CESAR BORDENAVE; ANDRES GARRIZ; CAROLINA GRANADOS MENDOZA; ANDRES ALBERTO RODRIGUEZ; JUAN FRANCISCO GIMENEZ-BREMONT
Congreso; XXXII Reunión Argentina de Fisiología Vegetal (RAFV) y XV Congreso Latinoamericano de Fisiología Vegetal; 2018
The polyamine oxidases (PAOs) catabolize the oxidative deamination of the polyamines (PAs) spermine (Spm) and spermidine (Spd). Most ofthe phylogenetic studies performed to analyze the plant PAO family took into account only a limited number and/or taxonomic representationof plant PAOs sequences. Here, we constructed a plant PAO protein sequence database and identified five subfamilies. Phylogeneticanalyses of these subfamilies revealed the existence of orthologs in Amborella trichopoda, suggesting that the earliest angiosperms werealready equipped with a broad set of PAOs, some of them lost subsequently during the evolution of the main angiosperm lineages. On thebases of known PAO protein structures, we performed a homology-modeling structure analysis. The comparison of the conserved aminoacids on the active site suggested that the presence of Glu to interact with the N5 of the substrate might be a critical factor determining theaccommodation of the substrate leading to a terminal catabolism (TC) type reaction mode. Moreover, the presence of either a His or anuncharged residue instead of Glu might lead to a back conversion (BC) type reaction mode. These results revealed that plant PAO family isbigger than previously conceived and present information for future structure-function and evolutionary.