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Literature summary extracted from
- Distinct gate conformations of the ABC transporter BtuCD revealed by electron spin resonance spectroscopy and chemical cross-linking (2009), FEBS Lett., 583, 266-270.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 7.6.2.8 | genes btuC and btuD form a cluster, encoding permease protein btuC and ATP-binding protein btuD, forming the ABC transporter BtuCD, expression of wild-type and utant enzymes as His-tagged proteins | Escherichia coli |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 7.6.2.8 | crystal structure analysis of the crystal structure of the BtuCD-F complex, modelling, overview | Escherichia coli |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 7.6.2.8 | S141C | site-directed mutagenesis, structure analysis | Escherichia coli |
| 7.6.2.8 | S143C | site-directed mutagenesis, structure analysis | Escherichia coli |
| 7.6.2.8 | T168C | site-directed mutagenesis, structure analysis | Escherichia coli |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 7.6.2.8 | membrane | periplasmic and cytosolic orientation | Escherichia coli | 16020 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.6.2.8 | Mg2+ | required | Escherichia coli |  |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.6.2.8 | ATP + H2O + vitamin B12/out | Escherichia coli | BtuCD is a type II ABC importer that catalyzes the translocation of vitamin B12 from the periplasm into the cytoplasm of Escherichia coli. BtuD is complexed with BtuC, a permease protein, and BtuF, a periplasmic binding protein, structure, overview | ADP + phosphate + vitamin B12/in | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.6.2.8 | Escherichia coli | P06611 | BtuD; gene btuD | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 7.6.2.8 | recombinant His-tagged wild-type and mutant enzymes by nickel affinity chromatography | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.6.2.8 | ATP + H2O + vitamin B12/out | - |
Escherichia coli | ADP + phosphate + vitamin B12/in | - |
? | |
| 7.6.2.8 | ATP + H2O + vitamin B12/out | BtuCD is a type II ABC importer that catalyzes the translocation of vitamin B12 from the periplasm into the cytoplasm of Escherichia coli. BtuD is complexed with BtuC, a permease protein, and BtuF, a periplasmic binding protein, structure, overview | Escherichia coli | ADP + phosphate + vitamin B12/in | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 7.6.2.8 | More | crystal structure analysis for conformations of the transmembrane domains that form inner and outer gates, structure comparison, overview | Escherichia coli |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.6.2.8 | BtuCD | - |
Escherichia coli |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 7.6.2.8 | 22 | - |
assay at | Escherichia coli |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 7.6.2.8 | 7.5 | - |
assay at | Escherichia coli |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.6.2.8 | ATP | - |
Escherichia coli | |
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Release 2023.1 (January 2023)
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