Cloned (Comment) | Organism |
---|---|
genes FN1863 and FN1862 encoding the alpha- and beta-subunit, respectively, recombinant expression in Escherichia coli strain Rosetta(DE3) pLysS | Fusobacterium nucleatum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(3S)-3,6-diaminohexanoate | Fusobacterium nucleatum | - |
(3S,5S)-3,5-diaminohexanoate | - |
r | |
D-lysine | Fusobacterium nucleatum | - |
2,5-diaminohexanoate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Fusobacterium nucleatum | Q8RHX7 AND Q8RHX8 | alpha- and beta-subunits | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(3S)-3,6-diaminohexanoate | - |
Fusobacterium nucleatum | (3S,5S)-3,5-diaminohexanoate | - |
r | |
D-lysine | - |
Fusobacterium nucleatum | 2,5-diaminohexanoate | - |
r | |
additional information | lysine 5,6-aminomutase (5,6-LAM) can perform 1,2-amino shifts on L-beta-lysine as well as D- and L-lysine. Docking of L-lysine or L-beta-lysine into the active site of 5,6-LAM revealed distinct non-covalent interactions between the substrate and the enzyme compared to that of the ornithine 4,5-aminomutase (EC 5.4.3.5) substrate complex. In 5,6-LAM, K370alpha forms a salt bridge with the alpha-carboxylate of the lysyl-pyridoxal 5'-phosphate complex, while the alpha-amine interacts with D298alpha. These two substitutions presumably increase the binding cavity of 5,6-LAM to accommodate different isomers of lysine. 5,6-LAM is able to act on D-lysine | Fusobacterium nucleatum | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
heterotetramer | alpha2beta2 | Fusobacterium nucleatum |
Synonyms | Comment | Organism |
---|---|---|
LAM | - |
Fusobacterium nucleatum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Fusobacterium nucleatum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.5 | - |
assay at | Fusobacterium nucleatum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
5'-deoxyadenosylcobalamin | - |
Fusobacterium nucleatum | |
additional information | lysine 5,6-aminomutase is a 5'-deoxyadenosylcobalamin and pyridoxal 5'-phosphate co-dependent radical enzyme | Fusobacterium nucleatum | |
pyridoxal 5'-phosphate | the protonation state of the pyridoxal 5'-phosphate cofactor has less of a role in radical-mediated chemistry compared to electrostatic interactions between the substrate and protein. Binding structure analysis and comparison with ornithine 4,5-aminomutase, EC 5.4.3.5 | Fusobacterium nucleatum |
General Information | Comment | Organism |
---|---|---|
additional information | lysine 5,6-aminomutase (5,6-LAM) from Clostridium sticklandii is an adenosylcobalamin (AdoCbl) and pyridoxal 5'-phosphate (PLP)-dependent enzyme | Fusobacterium nucleatum |