ArticleAngewandte Chemie (International ed. in English)2017
From Genome to Proteome to Elucidation of Reactions for All Eleven Known Lytic Transglycosylases from Pseudomonas aeruginosa.
Article in Angewandte Chemie (International ed. in English), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
38 citing papers in PubMed, 58 citations in OpenAlex.
- Denuded peptidoglycan oligosaccharides enable the biochemical investigation of bacterial cell wall recognition, modification, and degradation.The Journal of biological chemistry · 2026Article
- Outer Membrane-Peptidoglycan Anchoring inJournal of the American Chemical Society · 2026Article
- Article
- Structural Characterization of Lytic Transglycosylase SltB2 ofACS omega · 2025Article
- Reactions of SleC, Its Structure and Inhibition in Mitigation of Spore Germination inJournal of the American Chemical Society · 2025Article
- Editorial: Reviews in microbial pathogenesis.Frontiers in microbiology · 2025Article
- Structure of MltG from Mycobacterium abscessus reveals structural plasticity between composed domains.IUCrJ · 2024Article
- Lytic transglycosylase Slt of Pseudomonas aeruginosa as a periplasmic hub protein.Protein science : a publication of the Protein Society · 2024Article
- Structural characterization of lytic transglycosylase MltD of Pseudomonas aeruginosa, a target for the natural product bulgecin A.International journal of biological macromolecules · 2024Article
- Amber-codon suppression for spatial localization and in vivo photoaffinity capture of the interactome of the Pseudomonas aeruginosa rare lipoprotein A lytic transglycosylase.Protein science : a publication of the Protein Society · 2023Article
- Application of 2D-ITC to the Elucidation of the Enzymatic Mechanism ofBiochemistry · 2023Article
- Masters of Misdirection: Peptidoglycan Glycosidases in Bacterial Growth.Journal of bacteriology · 2023Review
- Hijacking the Peptidoglycan Recycling Pathway of Escherichia coli to Produce Muropeptides.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- In vitro studies of the protein-interaction network of cell-wall lytic transglycosylase RlpA of Pseudomonas aeruginosa.Communications biology · 2022Article
- Elucidation of host and symbiont contributions to peptidoglycan metabolism based on comparative genomics of eight aphid subfamilies and their Buchnera.PLoS genetics · 2022Article
- Peptidoglycan enzymes ofFrontiers in microbiology · 2022Review
- Molecular basis of dimerization of lytic transglycosylase revealed by the crystal structure of MltA fromIUCrJ · 2021Article
- Biochemical reconstitution defines new functions for membrane-bound glycosidases in assembly of the bacterial cell wall.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Turnover Chemistry and Structural Characterization of the Cj0843c Lytic Transglycosylase ofBiochemistry · 2021Article
- Unconventional Antibacterials and Adjuvants.Accounts of chemical research · 2021Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
An enzyme superfamily, the lytic transglycosylases (LTs), occupies the space between the two membranes of Gram-negative bacteria. LTs catalyze the non-hydrolytic cleavage of the bacterial peptidoglycan cell-wall polymer. This reaction is central to the growth of the cell wall, for excavating the cell wall for protein insertion, and for monitoring the cell wall so as to initiate resistance responses to cell-wall-acting antibiotics. The nefarious Gram-negative pathogen Pseudomonas aeruginosa encodes eleven LTs. With few exceptions, their substrates and functions are unknown. Each P. aeruginosa LT was expressed as a soluble protein and evaluated with a panel of substrates (both simple and complex mimetics of their natural substrates). Thirty-one distinct products distinguish these LTs with respect to substrate recognition, catalytic activity, and relative exolytic or endolytic ability. These properties are foundational to an understanding of the LTs as catalysts and as antibiotic targets.
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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.