TY  - BOOK
AU  - Amin Nur Husna Binti Airol Azamir
TI  - In silico characterization of phenylacetaldehyde synthases of selected orchids
SN  - THE0010286 (Local)
PY  - 2025///
CY  - Kuantan, Pahang
PB  - UMPSA
KW  - Faculty of Industrial Sciences and Technology
KW  - Dissertations
KW  - Universities and colleges
KW  - Final Year Report
N1  - Faculty of Industrial Sciences and Technology; Final Year Report (Bachelor of Applied Science in Industrial Biotechnology) -- Universiti Malaysia Pahang Al-Sultan Abdullah - 2025; Include bibliographical reference
N2  - Phenylacetaldehyde synthase (PAAS) is an enzyme essential for producing  phenylacetaldehyde, a key component of floral scent. It acts as a bifunctional enzyme,  efficiently coupling phenylalanine decarboxylation to oxidation. This process yields  phenylacetaldehyde, CO2, ammonia, and hydrogen peroxide in precise stoichiometric  amounts. Despite its importance, the presence and characteristics of PAAS in various  flowers remain underexplored. This study investigated the phenylacetaldehyde synthase  (PAAS) and its homologous proteins in five orchid species: Vanda Mimi Palmer, Phalaenopsis equestris, Dendrobium nobile, Dendrobium candidum, and Iris pallida,  using an in silico approach. Amino acid sequences available in the NCBI GenBank were  utilized to perform homology modeling and predict PAAS's three-dimensional (3D)  structures and related proteins. The reliability of these structural models was validated  using VERIFY 3D, PROCHECK, and ERRAT tools. This study aims to predict the 3Dprotein structure of selected orchids’ phenylacetaldehyde synthase and homologous  proteins using a homology modeling approach and to investigate the binding positions of  potential ligands to the 3D structure of the selected orchids’ phenylacetaldehyde  synthases by molecular docking. Active pocket regions (R1 and R2) were identified using  CASTp, whereas R1 is the predicted pocket binding site of the selected orchid  phenylacetaldehyde synthase and homologous proteins while R2 is the predicted pocket  binding site of the 6eem, and molecular docking experiments were conducted to evaluate  the binding sites and affinities of potential substrates (phenylalanine, tryptophan, and  tyrosine) and their products (phenylacetaldehyde, tryptamine, and tyramine). Finally,  protein-ligand docking studies were conducted with Autodock Vina to predict the  orientation of a ligand bound to the protein and compare it with the predicted active site  pocket analysis. This study contributes to a deeper understanding of PAAS's molecular  and functional properties and its homologous proteins in orchids. These insights enhance  knowledge of floral scent biosynthesis, particularly the enzymatic pathways involving  phenylacetaldehyde synthase, and provide valuable information for potential applications  in horticulture, the fragrance industry, and related fields
UR  - http://umpir.ump.edu.my/id/eprint/45596
ER  -