EC Number | Cloned (Comment) | Organism |
---|---|---|
1.16.3.1 | expressed in Escherichia coli | Mycobacterium tuberculosis |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.16.3.1 | determined at 3 A. The crystallographic data implicate the importance of the extended C-terminal region in the iron entry from the three-fold channels to the ferroxidase centre and making iron more readily accessible for the oxidation | Mycobacterium tuberculosis |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.16.3.1 | additional information | a truncated protein (having 1-167 amino acids, molecular weight ,18 kDa) is generated: The truncated protein shows a 3.5fold reduction in the oxidation rate of Fe(II). Lack of C-terminus has an impact of the stability of the protein. Truncated BfrB starts unfolding on exposure to even a very low temperature of 30°C whereas the native protein remains almost unaffected till 50°C before denaturing rapidly | Mycobacterium tuberculosis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.16.3.1 | Mycobacterium tuberculosis | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.16.3.1 | using NH4SO4 precipitation and gel filtration | Mycobacterium tuberculosis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.16.3.1 | 4 Fe2+ + 4 H+ + O2 | - |
Mycobacterium tuberculosis | 4 Fe3+ + 2 H2O | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.16.3.1 | bacterioferritin B | - |
Mycobacterium tuberculosis |
1.16.3.1 | BfrB | - |
Mycobacterium tuberculosis |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.16.3.1 | 30 | - |
truncated BfrB starts unfolding on exposure to even a very low temperature of 30°C whereas the native protein remains almost unaffected till 50°C before denaturing rapidly | Mycobacterium tuberculosis |