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Literature summary for 2.7.1.197 extracted from

  • Lolkema, J.; Robillard, G.
    Subunit structure and activity of the mannitol-specific enzyme II of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system solubilized in detergent (1990), Biochemistry, 29, 10120-10125.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Mg2+ Mg2+ ions at sufficiently high concentrations (5 mM) inhibit enzyme Escherichia coli
phosphate a 5fold dilution of a mixture of 10 mM phosphate, 5 mM MgSO4, and 50 mM NaF into phosphate buffers, pH 6.0-6.3 just before the zero time point leads to a rapid inhibition of the enzyme activity Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ Mg2+ ions bind specifically to enzyme, inducing dimerization Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1] Escherichia coli
-
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
r
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1] Escherichia coli ML308-225
-
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
r

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli ML308-225
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
-
Escherichia coli [protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
r
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
-
Escherichia coli ML308-225 [protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
r

Subunits

Subunits Comment Organism
dimer
-
Escherichia coli

Synonyms

Synonyms Comment Organism
IImtl
-
Escherichia coli
mannitol-specific enzyme I1
-
Escherichia coli