Reassessing the substrate specificities of the major Staphylococcus aureus peptidoglycan hydrolases lysostaphin and LytM
Lina Antenucci, Salla Virtanen, Chandan Thapa, Minne Jartti, Ilona Pitkänen, Helena Tossavainen, Perttu Permi, Volker Dötsch, Lina Antenucci, Salla Virtanen, Chandan Thapa, Minne Jartti, Ilona Pitkänen, Helena Tossavainen, Perttu Permi · 2024
Read Reassessing the substrate specificities of the major Staphylococcus aureus peptidoglycan hydrolases lysostaphin and LytM by Lina Antenucci, Salla Virtanen, Chandan Thapa, Minne Jartti, Ilona Pitkänen, Helena Tossavainen, Perttu Permi, Volker Dötsch, Lina Antenucci, Salla Virtanen, Chandan Thapa, Minne Jartti, Ilona Pitkänen, Helena Tossavainen, Perttu Permi (2024) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-11534333.txt.
Description
Bacteria that build and trim their own walls must cut the mesh at exactly the right bonds. Lina Antenucci and co-authors re-examined two wall-cutting enzymes of the staph bacterium in 2024, using nuclear magnetic resonance to watch which bonds each one actually breaks. One enzyme, lysostaphin, is itself a bacteria killer used against staph.
The two enzymes, close cousins in structure, turned out to share a taste for the same cross-linked part of the mature wall, contrary to earlier reports. Lysostaphin proved to be strictly a cutter of glycine-glycine links. Its cousin could also cut a neighboring bond type, making it a two-mode enzyme. The results give hard evidence for how this enzyme family earns its keep.
Catalog record
| CREATOR | Lina Antenucci, Salla Virtanen, Chandan Thapa, Minne Jartti, Ilona Pitkänen, Helena Tossavainen, Perttu Permi, Volker Dötsch, Lina Antenucci, Salla Virtanen, Chandan Thapa, Minne Jartti, Ilona Pitkänen, Helena Tossavainen, Perttu Permi |
|---|---|
| YEAR | 2024 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 79 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |