Gamma-D-glutamyl-meso-diaminopimelic acid peptidase (DL-peptidase)

DL-peptidase, specifically gamma-D-glutamyl-meso-diaminopimelic acid peptidase, is a specialized bacterial enzyme involved in the remodeling and degradation of the peptidoglycan layer. It catalyzes the hydrolysis of the peptide bond between the gamma-carboxyl group of D-glutamate and the L-amino group of meso-diaminopimelic acid (m-DAP), a critical cross-linking point in the cell walls of many bacteria, including Mycobacterium tuberculosis. This enzyme is a primary target for a novel class of antibacterial agents known as endolysins or enzybiotics, which are derived from bacteriophages. By targeting this specific bond, these therapeutic proteins can rapidly destabilize the bacterial cell wall, leading to osmotic lysis and cell death. DL-peptidase is particularly significant in the context of mycobacterial infections, where the unique structure of the cell wall requires specialized hydrolases for effective disruption. Research into DL-peptidase inhibitors and lysin-based therapies aims to provide new treatments for multi-drug resistant infections, offering a mechanism of action distinct from traditional antibiotics.

Other names

gamma-D-Glu-m-DAP peptidaseD-glutamyl-L-diaminopimelic acid endopeptidaseDL-endopeptidaseN5 domaingamma-D-glutamyl-L-diaminopimelic acid endopeptidaseL-alanyl-D-isoglutaminyl-meso-diaminopimelic acid peptidase

Hydrolysis of the gamma-D-glutamyl-meso-diaminopimelic acid bond within the bacterial peptidoglycan, which destabilizes the cross-linked murein sacculus and leads to osmotic lysis of the bacterial cell.