ArticleJournal of bacteriology2010
Muropeptide rescue in Bacillus subtilis involves sequential hydrolysis by beta-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 85 citations in OpenAlex.
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- The phenotypic landscape of the model firmicuteProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Metabolic flexibility and an unusual route for peptidoglycan muramic acid recycling in mycobacteria.The Journal of biological chemistry · 2026Article
- Denuded peptidoglycan oligosaccharides enable the biochemical investigation of bacterial cell wall recognition, modification, and degradation.The Journal of biological chemistry · 2026Article
- Post-translational modifications of GlmR integrate metabolic and stress signals to maintain cell envelope homeostasis in Bacillus subtilis.PLoS genetics · 2026Article
- Impairment of two non-essential LytR-cpsA-psr (Lcp) cell wall ligases decelerate cell wall assembly in Mycolicibacterium smegmatis.BMC microbiology · 2026Article
- Highly efficient chitinase production fromFrontiers in microbiology · 2026Article
- Staying in the loop to make ends meet: roles and regulation of GlmR inbioRxiv : the preprint server for biology · 2025Article
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- Characterization of psychrotrophic and thermoduric bacteria in raw milk using a multi-omics approach.Microbial genomics · 2024Article
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- Functional characterization of the phosphotransferase system in Parageobacillus thermoglucosidasius.Scientific reports · 2023Article
- Bacterial chitinases: genetics, engineering and applications.World journal of microbiology & biotechnology · 2022Review
- NamZ1 and NamZ2 from the Oral Pathogen Tannerella forsythia Are Peptidoglycan Processing Exo-β-Journal of bacteriology · 2022Article
- Genome sequencing and identification of cellulase genes in Bacillus paralicheniformis strains from the Red Sea.BMC microbiology · 2021Article
- A multistrategy approach for improving the expression of E. coli phytase in Pichia pastoris.Journal of industrial microbiology & biotechnology · 2020Article
- Utilization of different MurNAc sources by the oral pathogen Tannerella forsythia and role of the inner membrane transporter AmpG.BMC microbiology · 2020Article
- Characterization and diversity of the complete set of GH family 3 enzymes from Rhodothermus marinus DSM 4253.Scientific reports · 2020Article
- Examining the molecular characteristics of glycoside hydrolase family 20 β-N-acetylglucosaminidases with high activity.Bioengineered · 2019Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We identified a pathway in Bacillus subtilis that is used for recovery of N-acetylglucosamine (GlcNAc)-N-acetylmuramic acid (MurNAc) peptides (muropeptides) derived from the peptidoglycan of the cell wall. This pathway is encoded by a cluster of six genes, the first three of which are orthologs of Escherichia coli genes involved in N-acetylmuramic acid dissimilation and encode a MurNAc-6-phosphate etherase (MurQ), a MurNAc-6-phosphate-specific transcriptional regulator (MurR), and a MurNAc-specific phosphotransferase system (MurP). Here we characterized two other genes of this cluster. The first gene was shown to encode a cell wall-associated beta-N-acetylglucosaminidase (NagZ, formerly YbbD) that cleaves the terminal nonreducing N-acetylglucosamine of muropeptides and also accepts chromogenic or fluorogenic beta-N-acetylglucosaminides. The second gene was shown to encode an amidase (AmiE, formerly YbbE) that hydrolyzes the N-acetylmuramyl-L-Ala bond of MurNAc peptides but not this bond of muropeptides. Hence, AmiE requires NagZ, and in conjunction these enzymes liberate MurNAc by sequential hydrolysis of muropeptides. NagZ expression was induced at late exponential phase, and it was 6-fold higher in stationary phase. NagZ is noncovalently associated with lysozyme-degradable particulate material and can be released from it with salt. A nagZ mutant accumulates muropeptides in the spent medium and displays a lytic phenotype in late stationary phase. The evidence for a muropeptide catabolic pathway presented here is the first evidence for cell wall recovery in a Gram-positive organism, and this pathway is distinct from the cell wall recycling pathway of E. coli and other Gram-negative bacteria.
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