Structure and function of L,D- and D,D-transpeptidase family enzymes from Mycobacterium tuberculosis

(E-pub Abstract Ahead of Print)

Author(s): Gideon F. Tolufashe, Victor T. Sabe, Colins U. Ibeji, Thandokuhle Ntombela, Thavendran Govender, Glenn E. M. Maguire, Hendrik G. Kruger, Gyanu Lamichhane, Bahareh Honarparvar*.

Journal Name: Current Medicinal Chemistry


Peptidoglycan, the exoskeleton of bacterial cell and an essential barrier that protects the cell, is synthesized by a pathway whose final steps are catalysed by transpeptidases, including M.tuberculosis. Knowledge of the structure and function of these vital enzymes that generate this macromolecule in M. tuberculosis could facilitate the development of potent lead compounds against tuberculosis. This review summarizes the experimental and computational studies to date on these aspects of transpeptidases in M. tuberculosis that have been identified and validated. The reported structures of L,D- and D,D-transpeptidases, as well as their functionalities, are reviewed and the proposed enzymatic mechanisms for L,D-transpeptidases are summarized. In addition, we provide bioactivities of known M. tuberculosis drugs against these enzymes based on both experimental and computational approaches. Advancing knowledge about these prominent targets in M. tuberculosis supports the development of new drugs with novel inhibition mechanisms overcoming to address current need for new drugs against tuberculosis.

Keywords: Mycobacterium tuberculosis (Mtb), Peptidoglycan, L, D-transpeptidase, D, D-transpeptidase.

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(E-pub Abstract Ahead of Print)
DOI: 10.2174/0929867326666181203150231
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