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Conformational stability changes of the amino terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate: sugar phosphotransferase system produced by substituting alanine or glutamate for the active-site histidine 189: implications for phosphorylation effects.
The amino terminal domain of enzyme I (residues 1-258 + Arg; EIN) and full length enzyme I (575 residues; EI) harboring active-site mutations (H189E, expected to have properties of phosphorylated forms, and H189A) have been produced by protein bioengineering. Differential scanning calorimetry (DSC)...
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| Autors principals: | , , , , , , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
Cold Spring Harbor Laboratory Press
2000
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2144657/ https://ncbi.nlm.nih.gov/pubmed/10892802 |
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