Phylogenetic and Biochemical Analyses of Mycobacterial l,d-Transpeptidases Reveal a Distinct Enzyme Class That Is Preferentially Acylated by Meropenem.

ABSTRACT: The genomes of diverse mycobacterial species encode multiple proteins with the canonical l,d-transpeptidase (Ldt) sequence motif. The reason for this apparent redundancy is not well understood, but evidence suggests paralogous Ldts may serve niche roles in maintaining and/or remodeling mycobacterial peptidoglycan. We examined 323 mycobacterial Ldts and determined these enzymes cluster into six clades. We identified a variably represented yet distinct Ldt class (class 6) containing Mycobacterium smegmatis (Msm) LdtF and built a homology model of Msm LdtF toward elucidating class 6 structural and functional differences. We report class 6 Ldts have structurally divergent catalytic domains containing a 10-residue insertion near the active site and additionally determined t

SUBMITTER: Zandi TA 

PROVIDER: S-EPMC6910976 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature