The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Bacterial peptidoglycan (murein) hydrolases
Open accessAbstract
Most bacteria have multiple peptidoglycan hydrolases capable of cleaving covalent bonds in peptidoglycan sacculi or its fragments. An overview of the different classes of peptidoglycan hydrolases and their cleavage sites is provided. The physiological functions of these enzymes include the regulation of cell wall growth, the turnover of peptidoglycan during growth, the separation of daughter cells during cell division and autolysis. Specialized hydrolases enlarge the pores in the peptidoglycan for the assembly of large trans-envelope complexes (pili, flagella, secretion systems), or they specifically cleave peptidoglycan during sporulation or spore germination. Moreover, peptidoglycan hydrolases are involved in lysis phenomena such as fratricide or developmental lysis occurring in bacterial populations. We will also review the current view on the regulation of autolysins and on the role of cytoplasm hydrolases in peptidoglycan recycling and induction of beta-lactamase.
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Cites
Heilmann, C., Hussain, M., Peters, G., & Götz, F. (1997) · Molecular Microbiology · doi:10.1046/j.1365-2958.1997.4101774.x · Cited by 700
Use of bacteriolytic enzymes in determination of wall structure and their role in cell metabolism
Ghuysen, J. M. (1968) · Bacteriological Reviews · doi:10.1128/mmbr.32.4_pt_2.425-464.1968 · Cited by 569
Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli
Vollmer, W., & Bertsche, U. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.06.007 · Cited by 451
Self-citationHeidrich, C., Ursinus, A., Berger, J., Schwarz, H., & Höltje, J.-V. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.22.6093-6099.2002 · Cited by 272
Cited by
The abundance and variety of carbohydrate-active enzymes in the human gut microbiota
Kaoutari, A. E., Armougom, F., Gordon, J. I., Raoult, D., & Henrissat, B. (2013) · Nature Reviews Microbiology · doi:10.1038/nrmicro3050 · Cited by 1,683
Cross-biome metagenomic analyses of soil microbial communities and their functional attributes
Fierer, N., Leff, J. W., Adams, B. J., Nielsen, U. N., Bates, S. T., Lauber, C. L., Owens, S., Gilbert, J. A., Wall, D. H., & Caporaso, J. G. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1215210110 · Cited by 1,643
The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis
Sauvage, E., Kerff, F., Terrak, M., Ayala, J. A., & Charlier, P. (2008) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2008.00105.x · Cited by 1,317
Self-citationType VI secretion delivers bacteriolytic effectors to target cells
Russell, A. B., Hood, R. D., Bui, N. K., LeRoux, M., Vollmer, W., & Mougous, J. D. (2011) · Nature · doi:10.1038/nature10244 · Cited by 710
Self-citationExplosive cell lysis as a mechanism for the biogenesis of bacterial membrane vesicles and biofilms
Turnbull, L., Toyofuku, M., Hynen, A. L., Kurosawa, M., Pessi, G., Petty, N. K., Osvath, S. R., Cárcamo-Oyarce, G., Gloag, E. S., Shimoni, R., et al. (2016) · Nature Communications · doi:10.1038/ncomms11220 · Cited by 709
Metadata
- Authors
- Vollmer, W., Joris, B., Charlier, P., & Foster, S.
- Venue
- FEMS Microbiology Reviews
- Publisher
- Oxford University Press (OUP)
- Published
- 2008-03
- Volume
- 32
- Issue
- 2
- Pages
- 259-286
- ISSN
- 0168-6445 (ISSN-L)
- 1574-6976
- OpenAlex
- W2149941565
- Cited by
- 886
- References
- 4
- FWCI
- 24.78
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Vollmer, W., Joris, B., Charlier, P., & Foster, S. (2008). Bacterial peptidoglycan (murein) hydrolases. FEMS Microbiology Reviews. https://doi.org/10.1111/j.1574-6976.2007.00099.x
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
