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Literature summary extracted from

  • Sugiyama, S.; Vassylyev, D.G.; Matsushima, M.; Kashiwagi, K.; Igarashi, K.; Morikawa, K.
    Crystal structure of potD, the primary receptor of the poylamine transport system in Escherichia coli (1996), J. Biol. Chem., 271, 9519-9525.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
7.6.2.11
-
Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.6.2.11 periplasm PotD is a periplasmic binding protein Escherichia coli
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.6.2.11 additional information Escherichia coli Pot D is the primary receptor of the polyamine transport system, which regulates the polyamine content in E. coli ?
-
?

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.6.2.11 additional information Pot D is the primary receptor of the polyamine transport system, which regulates the polyamine content in E. coli Escherichia coli ?
-
?
7.6.2.11 spermidine/out + ATP + H2O
-
Escherichia coli spermidine/in + ADP + phosphate
-
?

Subunits

EC Number Subunits Comment Organism
7.6.2.11 More the PotD protein consists of two domains with an alterating beta-alpha-beta topology Escherichia coli
7.6.2.11 More the enzyme is a ATP-binding cassette transporter Escherichia coli