Literature summary extracted from
Frey, P.A.; Reed, G.H.
Lysine 2,3-aminomutase and the mechanism of the interconversion of lysine and beta-lysine (1993), Adv. Enzymol. Relat. Areas Mol. Biol., 66, 1-39.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
5.4.3.2 |
S-adenosylmethionine |
required |
Clostridium sp. |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
5.4.3.2 |
Co2+ |
enzyme bound cofactor |
Clostridium sp. |
|
5.4.3.2 |
Fe2+ |
Fe-S cluster is required as cofactor |
Clostridium sp. |
|
5.4.3.2 |
Fe2+ |
12 gatom of iron and of sulfide per mol of hexameric enzyme |
Clostridium sp. |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
5.4.3.2 |
Clostridium sp. |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
5.4.3.2 |
- |
Clostridium sp. |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
5.4.3.2 |
L-lysine = (3S)-3,6-diaminohexanoate |
mechanism |
Clostridium sp. |
|
5.4.3.2 |
L-lysine = (3S)-3,6-diaminohexanoate |
formation of substrate radicals as intermediates |
Clostridium sp. |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
5.4.3.2 |
L-Lys |
- |
Clostridium sp. |
(3S)-3,6-diaminohexanoic acid |
- |
? |
|
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
5.4.3.2 |
pyridoxal 5'-phosphate |
required |
Clostridium sp. |
|
5.4.3.2 |
pyridoxal 5'-phosphate |
contains 5.5 mol of pyridoxal phosphate per mol of hexameric enzyme |
Clostridium sp. |
|