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Literature summary for 2.7.1.207 extracted from

  • Dills, S.S.; Schmidt, M.R.; Saier, M.H.
    Regulation of lactose transport by the phosphoenolpyruvate-sugar phosphotransferase system in membrane vesicles of Escherichia coli (1982), J. Cell. Biochem., 18, 239-244.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
D-lactate
-
Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
methyl alpha-glucoside
-
Escherichia coli
additional information substrates of the phosphotransferase system inhibit uptake of lactose. This inhibition is reversed by intravesicular (but not extravesicular) phosphoenolpyruvate. lactose uptake is also inhibited by enzyme IIIGlc preparations that are shocked into the vesicles, and this inhibition is reversed by phosphoenolpyruvate. Enzyme I and HPr neither inhibit nor stimulate lactose uptake Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[protein]-Npi-phospho-L-histidine + lactose[side 1] Escherichia coli
-
[protein]-L-histidine + lactose 6'-phosphate[side 2]
-
?
[protein]-Npi-phospho-L-histidine + lactose[side 1] Escherichia coli ML308-225
-
[protein]-L-histidine + lactose 6'-phosphate[side 2]
-
?

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 + lactose[side 1]
-
Escherichia coli [protein]-L-histidine + lactose 6'-phosphate[side 2]
-
?
[protein]-Npi-phospho-L-histidine + lactose[side 1]
-
Escherichia coli ML308-225 [protein]-L-histidine + lactose 6'-phosphate[side 2]
-
?

Synonyms

Synonyms Comment Organism
lactose permease
-
Escherichia coli