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Neutron structure of the T26H mutant of T4 phage lysozyme provides insight into the catalytic activity of the mutant enzyme and how it differs from that of wild type
T4 phage lysozyme is an inverting glycoside hydrolase that degrades the murein of bacterial cell walls by cleaving the β‐1,4‐glycosidic bond. The substitution of the catalytic Thr26 residue to a histidine converts the wild type from an inverting to a retaining enzyme, which implies that the original...
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| Veröffentlicht in: | Protein Sci |
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| Hauptverfasser: | , , , , , , |
| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
John Wiley and Sons Inc.
2017
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5606550/ https://ncbi.nlm.nih.gov/pubmed/28707339 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.3230 |
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