EC Number | Crystallization (Comment) | Organism |
---|---|---|
7.6.2.8 | BtuCD-F complex analyzed at a resolution of 2.6 A, substantial conformational changes observed as compared with previously reported structures of BtuCD and BtuF | Escherichia coli |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
7.6.2.8 | periplasm | - |
Escherichia coli | - |
- |
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 | - |
ADP + phosphate + vitamin B12/in | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
7.6.2.8 | Escherichia coli | P06611 | encoded by btuD gene | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
7.6.2.8 | additional information | - |
crystal structure of BtuCD-F complex presented, displacement of vitamin B12 from binding pocket shown, subunits of transmembrane BtuC protein shown to have two distinct conformations, translocation pathway shown to be closed to both sides of the membrane, electron paramagnetic resonance spectra of spin-labeled cysteine mutants shown to be consistent with the conformation of BtuCD-F observed in the crystal structure, structure of BtuCD-F discussed as a posttranslocation intermediate | Escherichia coli |
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 | crystal structure of BtuCD-F complex determined, BtuF protein shown to be bound to the periplasmic face of BtuCD | Escherichia coli | ADP + phosphate + vitamin B12/in | - |
? |