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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Main Authors: Ginsburg, A., Szczepanowski, R. H., Ruvinov, S. B., Nosworthy, N. J., Sondej, M., Umland, T. C., Peterkofsky, A.
Formáid: Artigo
Teanga:Inglês
Foilsithe: Cold Spring Harbor Laboratory Press 2000
Ábhair:
Research Article
Rochtain Ar Líne:https://ncbi.nlm.nih.gov/pmc/articles/PMC2144657/
https://ncbi.nlm.nih.gov/pubmed/10892802
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