Cloned (Comment) | Organism |
---|---|
expressed as a C-terminal Flag-tagged fusion protein | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Escherichia coli | BtuCD alone or the BtuCD-F complex do not bind vitamin B12. Only free, uncomplexed BtuF binds vitamin B12 with high affinity. Upon binding of BtuF to BtuCD, vitamin B12 is released from BtuF and is only transiently associated with the complex | ? | - |
? | |
additional information | Escherichia coli | BtuCD forms an extremely stable complex with the vitamin B12 binding protein BtuF. Vitamin B12 accelerates complex dissociation rate, with ATP having an additional destabilizing effecf | ? | - |
? | |
additional information | Escherichia coli | in the presence of vitamin B12, upon binding of ATP (or ATP analogues), no association between BtuF and BtuCD can be detected | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | BtuCD alone or the BtuCD-F complex do not bind vitamin B12. Only free, uncomplexed BtuF binds vitamin B12 with high affinity. Upon binding of BtuF to BtuCD, vitamin B12 is released from BtuF and is only transiently associated with the complex | Escherichia coli | ? | - |
? | |
additional information | BtuCD forms an extremely stable complex with the vitamin B12 binding protein BtuF. Vitamin B12 accelerates complex dissociation rate, with ATP having an additional destabilizing effecf | Escherichia coli | ? | - |
? | |
additional information | in the presence of vitamin B12, upon binding of ATP (or ATP analogues), no association between BtuF and BtuCD can be detected | Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
BtuCD vitamin B12 importer | - |
Escherichia coli |