Analysis of Suitable Signal Peptides for Secretion of a Recombinant Alcohol Dehydrogenase with a Key Role in Atorvastatin Enzymatic Synthesis

Overview

Journal Mol Biol Res Commun

Specialty Molecular Biology

Date 2019 Sep 19

PMID 31528640

Citations 6

Authors

Mortaza Taheri-Anganeh

Seyyed Hossein Khatami

Zeinab Jamali

Amir Savardashtaki

Younes Ghasemi

Zohreh Mostafavi-Pour

Affiliations

Soon will be listed here.

Abstract

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 alcohol dehydrogenase (LKADH). Therefore, recombinant enzyme secretion by 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.

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