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Literature summary extracted from

  • Abramson, J.; Kaback, H.R.; Iwata, S.
    Structural comparison of lactose permease and the glycerol-3-phosphate antiporter: members of the major facilitator superfamily (2004), Curr. Opin. Struct. Biol., 14, 413-419.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
7.6.2.10 X-ray structure, GlpT consists of 12 transmembrane helices, which form a N- and C-terminal domain, the structure reveals a large internal cavity, open toward the cytoplasm but completely closed to the periplasm, the substrate-binding site, formed by two arginine residues, is accessible from only one side of the membrane at a time Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.6.2.10 inner membrane
-
Escherichia coli
-
-

Organism

EC Number Organism UniProt Comment Textmining
7.6.2.10 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.6.2.10
-
Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.6.2.10 ATP + H2O + glycerol-3-phosphate/out
-
Escherichia coli ADP + phosphate + glycerol-3-phosphate/in
-
?

Synonyms

EC Number Synonyms Comment Organism
7.6.2.10 GlpT
-
Escherichia coli
7.6.2.10 glycerol-3-phosphate antiporter
-
Escherichia coli