PHYLOGENETIC ANALYSIS OF DELTA-GUAIENE SYNTHASE FROM AGARWOODPRODUCING PLANTS (AQUILARIA CRASSNA)
Aquilaria crassna is a member of the Thymelaeaceae, a plant that produces agarwood or resin that accumulates in plant tissues used for medicinal and perfumery purposes. One of the main components of gaharu production is deltaguaiene, a sesquiterpene compound synthesized by the activity of the enz...
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Format: | Final Project |
Language: | Indonesia |
Online Access: | https://digilib.itb.ac.id/gdl/view/63251 |
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Institution: | Institut Teknologi Bandung |
Language: | Indonesia |
Summary: | Aquilaria crassna is a member of the Thymelaeaceae, a plant that produces
agarwood or resin that accumulates in plant tissues used for medicinal and
perfumery purposes. One of the main components of gaharu production is deltaguaiene,
a sesquiterpene compound synthesized by the activity of the enzyme deltaguaiene
synthase (DGS). However, research on delta-guaiene synthase in Aquilaria
species is still minimal. The purpose of this study was to analyze the evolutionary
relationship of delta-guaiene synthase A. crassna (AcDGS) with sesquiterpene
synthase in the genus Aquilaria, as well as non-gaharu-producing species. A total
of 37 sesquiterpene synthase gene sequences from the National Center for
Biotechnology (NCBI) were used to reconstruct the phylogenetic tree. As an
outgroup, a sesquiterpene synthase from the monocot plant, Oryza barthii (ObSTS)
was used. Identification of positive selection sites was carried out to determine the
history of mutations in AcDGS. The analysis was continued by determining the
comparison of the AcDGS protein structure with the sesquiterpene synthase of the
4 selected species. Based on the phylogenetic tree, AcDGS forms a group with the
species Aquilaria, Stellera chamaejasme, Zanthoxylum piperitum, and Citrus
bergamia. Only 1 positive selection site was detected, Ser10 AcDGS. Mutations at
this site did not affect the protein's catalytic activity. The AcDGS protein analysis
found 2 terminal domains, 4 conserved motifs, and several functional sites. most of
the functional sites, such as aspartate-rich regions, active site cap residues, and
substrate-binding regions are located in the C-terminal domain. No functional sites
were found in the N-terminal domain. Comparison of the 3D structure of AcDGS
with other sesquiterpene synthases did not provide a significant difference. The
results of this study are expected to be used as a basis for molecular engineering in
the formation of agarwood.
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