Bioinformatics analysis of the key enzyme of important volatile phenylpropanoid pathway in Ocimum basilicum

Essential oils of O. basilicum are rich in phenylpropanes like chavicol, methylchavicol, eugenol,methyleugenol, and some terpenoid compounds, which are contributed to the particular properties of manyspices and herbs. The final step in the biosynthesis of the methylchavicol, the conversion of chavicol tomethylchavicol, is catalyzed by the enzyme chavicol O-methyltransferase (CVOMT). Here, we study thestructural and functional important regions (motif prediction), conserved domains, protein domain families,catalytic domains were detected in the protein sequence via PROSITE, InterProScan, ProDom, TrEMBL,respectively. PSORT Prediction, predict Nuclear Localization Signals (NLS) tool and Subcellular locationprediction (PLS) web tools. The ObCVOMT protein molecular mass was predicted to be about ۳۹.۹۵ kDaand the isoelectric point was predicted to be at ۵.۵۸ calculated. In addition, the putative amino acids sequencerevealed more homology with conserved active site consensus sequence of all the PAL protein conservedmotifs (MSLKCAIQLGIPDILHKHDHPMTLSQLLQAIPINKEKSQSFQRLMRALV), and belongs to theclass I-like SAM-binding methyltransferase superfamily and Cation-independent O-methyltransferasefamily. MotifScan results revealed that the protein sequence of ObCVOMT had ۱۱ catalytic domainsconsisting of eight different catalytic domains viz. ASN_GLYCOSYLATION (N-glycosylation site),CK۲_PHOSPHO_SITE (Casein kinase II phosphorylation site), MYRISTYL (N-myristoylation site).Results from protein structure modeling program SOPMA revealed that predicted ObCVOMT protein was apredominantly α-helical protein, which mainly consisted of alpha helices (۴۹.۱۶%) and random coils(۳۲.۰۲%), extended strands (۱۳.۴۸%), and ۵.۳۴% beta turns.

کلیدواژه ها:

ObCVOMT ، Catalytic domains ، Conserved domains ، protein structure modeling ، motif scan