Activating Compound | Comment | Organism | Structure |
---|---|---|---|
S-adenosylmethionine | required | Clostridium subterminale | |
S-adenosylmethionine | plays a role in lysine 2,3-aminomutase reaction | Clostridium subterminale |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | role of the iron-sulfur clusters in the reaction | Clostridium subterminale | |
Fe2+ | Fe-S cluster is required as cofactor | Clostridium subterminale |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Clostridium subterminale | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-lysine = (3S)-3,6-diaminohexanoate | reaction proceeds by a substrate radical rearrangement mechanism, in which the external aldimine formed between pyridoxal phosphate and Lys is initially converted into a lysyl-radical intermediate by hydrogen abstraction from C3 | Clostridium subterminale |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-Lys | - |
Clostridium subterminale | (3S)-3,6-diaminohexanoic acid | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | required | Clostridium subterminale | |
pyridoxal 5'-phosphate | role in lysine 2,3-aminomutase reaction | Clostridium subterminale |