Literature summary for 2.7.3.9 extracted from

Ginsburg, A.; Szczepanowski, R.H.; Ruvinov, S.B.; Nosworthy, N.J.; Sondej, M.; Umland, T.C.; Peterkofsky, A.
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 (2000), Protein Sci., 9, 1085-1094.

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Protein Variants

Protein Variants	Comment	Organism
H189A	thermodynamics	Escherichia coli
H189E	thermodynamics	Escherichia coli
additional information	N-terminal domain, thermodynamic properties	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

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Release 2023.1 (January 2023)