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Literature summary for 2.7.1.199 extracted from

  • Kalbermatter, D.; Chiu, P.L.; Jeckelmann, J.M.; Ucurum, Z.; Walz, T.; Fotiadis, D.
    Electron crystallography reveals that substrate release from the PTS IIC glucose transporter is coupled to a subtle conformational change (2017), J. Struct. Biol., 199, 39-45 .
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane integral membrane protein 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 + D-glucose[side 1] Escherichia coli the enzyme is highly stereoselective for its substrate D-glucose [protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P69783
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme does not bind L-glucose Escherichia coli ?
-
-
[protein]-Npi-phospho-L-histidine + D-glucose[side 1] the enzyme is highly stereoselective for its substrate D-glucose Escherichia coli [protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
 ?

Subunits

Subunits Comment Organism
homodimer x-ray crystallography Escherichia coli

Synonyms

Synonyms Comment Organism
glucose-specific EII complex
-
 Escherichia coli
IICB the glucose-specific phosphotransferase system includes the integral membrane protein IICB that couples the transmembrane transport of D-glucose to its phosphorylation Escherichia coli
IICglc glucose-specific IIC transport domain Escherichia coli
PTS IIC glucose transporter
-
 Escherichia coli