کنگره بین المللی زیست فناوری گیاهان دارویی و قارچ های کوهی

صفحه اصلی / چهارمین کنگره بین المللی و پنجمین همایش ملی زیست فناوری گیاهان دارویی و قارچ های کوهی

In silico analysis of the predicted protein sequence of linalool synthase as a key enzyme in the biosynthesis of linalool compound in Mentha citrata

نویسندگان :

Fatemeh Bikdeli¹ Fatemeh Khakdan²

1- دانشگاه تخصصی فناوری های نوین آمل 2- دانشگاه سمنان

کلمات کلیدی :

linalool synthase (Lins)،phylogenetic analysis،conserved domains،catalytic domains،motif prediction

چکیده :

Linalool is one of the most important compounds in the essential oil of Mentha citrate which, in addition to its use in various food and pharmaceutical industries, as well as in the treatment of cancer, having antiproliferative properties. Two basic precursors IPP and DMAPP, after the formation of GPP, by the enzyme linalool synthase (Lins) (the key and final enzyme of the pathway) move towards the production of linalool compound. Phylogenetic tree was classified into 3 clusters. McLins was found associated with Thymus vulgaris followed by Salvia miltiorrhiza. In addition, based on InterProScan tool and pfam database, the putative amino acids sequence revealed more homology with conserved active site consensus sequence at the N terminus of a variety of plant diterpenoid biosynthetic enzyme to mediate magnesium ion binding and lyase activity. PROSITE motif results exhibited that McLins have two major motifs, Terpene_synth_C, Terpene synthase family, and metal binding domain. Results showed that deduced McLins protein was a predominantly α-helical protein, which mainly consisted of alpha helix (63.86%), random coils (26.24%), extended strands (6.60%), and 3.30% beta turns.