EC Number | Crystallization (Comment) | Organism |
---|---|---|
5.4.99.1 | - |
Clostridium tetanomorphum |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
5.4.99.1 | 14800 | - |
2 * 14800, B12-binding component S, + 2 * 53700, component E | Clostridium tetanomorphum |
5.4.99.1 | 53700 | - |
2 * 14800, B12-binding component S, + 2 * 53700, component E | Clostridium tetanomorphum |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.4.99.1 | Clostridium tetanomorphum | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.4.99.1 | L-Glu | - |
Clostridium tetanomorphum | threo-3-Methylaspartate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
5.4.99.1 | tetramer | 2 * 14800, B12-binding component S, + 2 * 53700, component E | Clostridium tetanomorphum |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
5.4.99.1 | Cobalamin | dependent on | Clostridium tetanomorphum | |
5.4.99.1 | Cobalamin | the major part of component S is preorganized for vitamin B12 binding, but the B12-binding site itself is only partially formed. Upon binding B12, important elements of the binding site appear to become structured, including an alpha-helix that forms one side of the cleft accomodating the nucleotide 'tail' of the cofactor | Clostridium tetanomorphum |