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Literature summary for 7.6.2.11 extracted from
- Crystal structure of potD, the primary receptor of the poylamine transport system in Escherichia coli (1996), J. Biol. Chem., 271, 9519-9525.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| periplasm | PotD is a periplasmic binding protein | Escherichia coli | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Escherichia coli | Pot D is the primary receptor of the polyamine transport system, which regulates the polyamine content in E. coli | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Pot D is the primary receptor of the polyamine transport system, which regulates the polyamine content in E. coli | Escherichia coli | ? | - |
? | |
| spermidine/out + ATP + H2O | - |
Escherichia coli | spermidine/in + ADP + phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the PotD protein consists of two domains with an alterating beta-alpha-beta topology | Escherichia coli |
| More | the enzyme is a ATP-binding cassette transporter | Escherichia coli |
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