Bioinformatics Investigation of HMBPP Reductase Enzyme from Ocimum basilicum L.
- سال انتشار: 1397
- محل انتشار: دومین کنفرانس بین المللی فناوری های نوین در علوم
- کد COI اختصاصی: CMTS02_271
- زبان مقاله: انگلیسی
- تعداد مشاهده: 301
نویسندگان
Ph. D in Agricultural Biotechnology
Department of Biology, Faculty of Science, Yasouj University, Yasouj, Iran
Department of Microbial Biotechnology, Faculty of Biotechnology, Amol University of Special Modern Technologies, Amol, Iran
چکیده
Secondary metabolites of Ocimum basilicum L. exhibit substantial medicinal properties such as antimicrobial [1,2], antioxidant [3,4] and bactericidal properties [5,6]. Basil essential oil belongs to two major groups, monoterpene derivatives (e.g. camphor, linalool and, geraniol) and phenylpropanoid derivatives (e.g. eugenol, methyl eugenol and, chavicol) [1,7]. Linaool, the most important compound of basil essential oil, is synthesized by methylerythritol phosphate (MEP) pathway which occurs in the chloroplast. The 4-hydroxy-3-methylbut-2-enyl pyrophosphate (HMBPP) reductase (HRD, EC 1.17.7.4) is one of the key enzymes of the pathway that catalyzes HMBPP conversion into isopentenyl pyrophosphate (IPP) and dimethylallyl pyrophosphate (DMAPP) (precursors of isoprenoid compounds) [8]. We aimed to analyze ObHRD cDNA sequence (Gene bank accession number, KU375118) to obtain more detailed information of this enzyme. ORF finder, ScanSite, ProtParam, PROSITE, InterProScan, ProDom, TrEMBL programs were utilized for finding ORF, physicochemical properties, structural and functionally important regions of predicted HDR protein, respectively. ObHRD cDNA (1309 nt) had the start codon (ATG) and the stop codon (TAA) in 103 and 1017 positions, respectively. It encoded a 305 amino acid polypeptide which indicated high homology with other identified HRDs from Ocimum or even other genera. Molecular weight and pI of predicted protein were 73.52 kD and 5.16, respectively. The half-life of protein estimated more than 20 h and its instability index was 35.29, therefore, this protein could be classified as a stable protein. The most abundant amino acids of the enzyme were Ala (31.6%), Tyr (26.7%) Gly (26.3%) and, Cys (15.4%). The blast of ObHDR amino acid sequence showed high homology with other HDRs isolated from Salvia miltiorhiza (87%), Sesamum indicum (86%) and, Salvia miltiorhiza, b. alba (84%). PORTER program demonstrated that α-helices secondary structures comprised the most parts of the protein (40.46%) and residual parts divided into strings (20.27%), sheets (15.13%) and, random coils (23.68%). Subcellular position prediction showed that ObHRD had a 63 amino acid signal peptide at the N-terminal end for transporting to the plastid. N-terminal domain conserved at Cys 12, Cys 96 and Cys 167 positions and conserved Tyr 72 was critical for HDR function [9]. Variation of this domain could have important roles in Fe-S cluster formation, substrate binding and catalytic function of the enzyme [10]. Acquiring more knowledge about HDR enzyme could assist us for a better understanding of MEP pathway regulation mechanisms and even metabolic engineering of this pathway.کلیدواژه ها
Bioinformatics, HMBPP reductase, MEP pathway, Ocimum basilicum Lمقالات مرتبط جدید
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