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In silico analysis of suitable signal peptides for secretion of a recombinant alcohol dehydrogenase with a key role in atorvastatin enzymatic synthesis | ||
| Molecular Biology Research Communications | ||
| مقاله 3، دوره 8، شماره 1، 2019، صفحه 17-26 اصل مقاله (626.31 K) | ||
| نوع مقاله: Original article | ||
| شناسه دیجیتال (DOI): 10.22099/mbrc.2019.31801.1372 | ||
| نویسندگان | ||
| Mortaza Taheri1؛ Seyyed Hossein Khatami2؛ Zeinab Jamali3؛ Amir Savardashtaki1؛ Younes Ghasemi4، 5؛ Zohreh Mostafavipour* 2، 6 | ||
| 1Department of Medical Biotechnology, School of Advanced Medical Sciences and Technologies, Shiraz University of Medical Sciences, Shiraz, Iran | ||
| 2Recombinant Proteins Laboratory, Department of Biochemistry, School of Medicine, Shiraz University of Medical Sciences, Shiraz, Iran | ||
| 3Cardiovascular Research Center, Shiraz University of Medical Sciences, Shiraz, Iran | ||
| 4Department of Pharmaceutical Biotechnology, School of Pharmacy, Shiraz University of Medical Sciences, Shiraz, Iran | ||
| 5Pharmaceutical Sciences Research Center, Shiraz University of Medical Sciences, Shiraz, Iran | ||
| 6Maternal-Fetal Medicine Research Center, Shiraz University of Medical Sciences, Shiraz, Iran | ||
| چکیده | ||
| An elevated cholesterol level might lead to cardiovascular disease (CVD). Statins block the cholesterol synthesis pathway in the liver. Atorvastatin is the most widespread statin worldwide and, its chemical synthesis requires toxic catalysts, resulting in environmental pollution. Hence, enzymatic synthesis of atorvastatin is desirable. This process could be done by Lactobacillus kefir alcohol dehydrogenase (LKADH). Therefore, recombinant enzyme secretion by Escherichia coli using signal peptides (SPs) might result in easy production and purification. To achieve this objective, we used some online bioinformatics web servers to evaluate the suitable SPs for translocation of LKADH into extracellular spaces. “Signal Peptide Website” and “UniProt” were utilized to retrieve the SPs and LKADH sequences. “SignalP 4.1” was used to determine SPs and their cleavage site location and the results were rechecked by “Philius”. Physicochemical features of SPs were evaluated by “ProtParam”, then solubility of their fusion with LKADH was assessed by “Protein-sol”. Finally, secretion pathway and sub-cellular localization of the selected stable and soluble LKADH fusions were predicted by “PRED-TAT” and “ProtCompB”. Amongst the 41 evaluated SPs, only LPTA_ECOLI, SUBF_BACSU, CHIS_BACSU, SACB_BACAM, CDGT_BACST and AMY_BACLI could translocate LKADH out of cytoplasm. The six selected SPs in the result section were suitable to design a soluble secretory LKADH that accelerate its scale-up production and might be useful in future experimental researches. | ||
| کلیدواژهها | ||
| Atorvastatin؛ Alcohol dehydrogenase؛ Signal peptide؛ In silico | ||
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