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Structure-function relationships underlying the dual N-acetylmuramic and N-acetylglucosamine specificities of the bacterial peptidoglycan deacetylase PdaC
Bacillus subtilis PdaC (BsPdaC) is a membrane-bound, multidomain peptidoglycan N-deacetylase acting on N-acetylmuramic acid (MurNAc) residues and conferring lysozyme resistance to modified cell wall peptidoglycans. BsPdaC contains a C-terminal family 4 carbohydrate esterase (CE4) catalytic domain, b...
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| Gepubliceerd in: | J Biol Chem |
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| Hoofdauteurs: | , , , , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
American Society for Biochemistry and Molecular Biology
2019
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6916482/ https://ncbi.nlm.nih.gov/pubmed/31690626 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA119.009510 |
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