Abstract: Mycobacterium tuberculosis (Mtb) infects nearly ten million individuals worldwide every year and problem is even worst due to increase in number of multi drug resistance. Tuberculosis elimination program under National Strategic Plan need progressive studies on protein, enzyme and pathways of Mtb. This would facilitate the urgent need to design and development of additional novel/potent antitubercular agents. The Lysine/DAP biosynthetic pathway is a promising target as it finds specific role in cell wall and amino acid biosynthesis. In this study, we predominantly aimed an enzyme DapE from M. tuberculosis H37Rv (Mtb-DapE) consists of 354 amino acids with a theoretical molecular weight of 37,240 Daltons. Mtb-DapE gene was amplified and cloned into bacterial expression vectors. The recombinant DapE protein was successfully purified from inclusion bodies with a high yield. This structurally compatible well folded protein as assessed by the CD spectral analyses could thus be useful for advanced anti-tubercular targeting studies.
Keywords: Mycobacterium tuberculosis, Lysine/DAP biosynthetic pathway, DapE, Protein.
Title: Cloning, expression, and refolding of N-succinyl-l-l diaminopimelic acid desuccinylase (DapE) of Mycobacterium tuberculosis
Author: Chinmay P. Umbarkar, Prashant S. Thakre, Supriya A. Kashikar, Niraj A. Ghanwate, Vinod B. Agarkar
International Journal of Life Sciences Research
ISSN 2348-313X (Print), ISSN 2348-3148 (online)
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