ArticleBMC biochemistry2017
Structural insight into the inactivation of Mycobacterium tuberculosis non-classical transpeptidase Ldt
Article in BMC biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 50 citations in OpenAlex.
- Outer Membrane-Peptidoglycan Anchoring inJournal of the American Chemical Society · 2026Article
- Peptide Mimetic Platform for Activity Profiling of Mycobacterial l,d-Transpeptidases.Biochemistry · 2026Article
- Chemoproteomic Elucidation of β-Lactam Drug Targets inACS infectious diseases · 2026Article
- Activity Profiling of Mycobacterial L,D-Transpeptidases.bioRxiv : the preprint server for biology · 2026Article
- Recent advances in drug repositioning and rediscovery for different therapeutic activities utilizing updated technological approaches.Molecular diversity · 2026Review
- Peptidoglycan LD-Transpeptidases.Antibiotics (Basel, Switzerland) · 2025Review
- Biochemical and crystallographic studies of L,D-transpeptidase 2 from Mycobacterium tuberculosis with its natural monomer substrate.Communications biology · 2024Article
- The l,d-Transpeptidase LdtACS infectious diseases · 2022Article
- Structure-Activity Relationship of Penem Antibiotic Side Chains Used against Mycobacteria Reveals Highly Active Compounds.ACS infectious diseases · 2022Article
- T405, a New Penem, ExhibitsAntimicrobial agents and chemotherapy · 2022Article
- Article
- Studies on the Reactions of Biapenem with VIM Metallo β-Lactamases and the Serine β-Lactamase KPC-2.Antibiotics (Basel, Switzerland) · 2022Article
- Identification of β-Lactams Active againstACS infectious diseases · 2022Article
- Penicillin Binding Proteins and β-Lactamases of Mycobacterium tuberculosis: Reexamination of the Historical Paradigm.mSphere · 2022Article
- β-Lactam antibiotic targets and resistance mechanisms: from covalent inhibitors to substrates.RSC medicinal chemistry · 2021Review
- Structural and Cellular Insights into the l,d-Transpeptidase YcbB as a Therapeutic Target in Citrobacter rodentium,Antimicrobial agents and chemotherapy · 2021Article
- A Fluorescence-Based Assay for Screening β-Lactams Targeting the Mycobacterium tuberculosis Transpeptidase LdtChembiochem : a European journal of chemical biology · 2020Article
- Activity-Based Protein Profiling Reveals That Cephalosporins Selectively Active on Non-replicatingFrontiers in microbiology · 2020Article
- Phylogenetic and Biochemical Analyses of Mycobacterial l,d-Transpeptidases Reveal a Distinct Enzyme Class That Is Preferentially Acylated by Meropenem.ACS infectious diseases · 2019Article
- Identification of potent L,D-transpeptidase 5 inhibitors for Mycobacterium tuberculosis as potential anti-TB leads: virtual screening and molecular dynamics simulations.Journal of molecular modeling · 2019Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundThe carbapenem subclass of β-lactams is among the most potent antibiotics available today. Emerging evidence shows that, unlike other subclasses of β-lactams, carbapenems bind to and inhibit non-classical transpeptidases (L,D-transpeptidases) that generate 3 → 3 linkages in bacterial peptidoglycan. The carbapenems biapenem and tebipenem exhibit therapeutically valuable potencies against Mycobacterium tuberculosis (Mtb).
resultsHere, we report the X-ray crystal structures of Mtb L,D-transpeptidase-2 (Ldt
conclusionThe results presented here demonstrate biapenem and tebipenem bind to the outer cavity of Ldt
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.