Revista de química física y biofísica
Acceso abierto

abstracto

Análisis bioinformático de la fenilacetaldehído sintasa (PAAS), una proteína involucrada en la producción de aromas florales, en rosa

Akbar Karami Samira Jandoust y Esmaeil Ebrahimie

Rose flowers produce and emit the aromatic volatiles 2-phenylacetaldehyde (PAA) and 2-phenylethanol (2-PE), which have a distinctive flowery/rose-like scent. Previous studies of rose have shown that, similar to Petunia flowers, PAA is formed from L-phenylalanine via pyridoxal-5'-phosphate-dependent L-aromatic amino acid decarboxylase. Rosa phenylacetaldehyde synthase sequence (RhPAAS) is homologous to Petunia phenylacetaldehyde synthase (PhPAAS). Since there is not much experimental data available about different structural properties of that PAAS protein, in the present investigation, we studied the different structural properties of the PAAS protein in petunia and rose using bioinformatics tools. The features of the first, secondary and tertiary structures of this protein were compared between Petunia and Rose. The results indicated that the frequency of negatively charged, Leucine, and frequency of the Ser-Leu, Pro-Glu , Phe-Ser and the, Thr-Thr dipeptides in petunia are more than those in Rose. In contrast, in petunia, the frequencies of hydrophobic and hydrophilic residues, α-helix, β-sheet, β-strands of petunia are lower than those in rose. The features achieved in this study may also provide useful clues for designing scent production pathways using protein engineering techniques.