Protein Variants | Comment | Organism |
---|---|---|
E216Q | mutation increases the Km value for L-Lys by 30fold with very little change on the kcat value or in the binding of NAD(P)H | Nocardia farcinica |
M239R | mutation results in high production of hydrogen peroxide and little hydroxylation with no change in coenzyme selectivity | Nocardia farcinica |
R301A | mutation causes a 300fold decrease on kcat/Km value with NADPH but no change with NADH | Nocardia farcinica |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.08 | - |
NADPH | pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme M239R, determined by by measuring oxygen consumption | Nocardia farcinica | |
0.09 | - |
NADPH | pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme M239R, determined by by measuring oxygen consumption | Nocardia farcinica | |
0.14 | - |
NADPH | pH 7.5, 25°C, cosubstrate L-lysine, wild-type enzyme, determined by by measuring oxygen consumption | Nocardia farcinica | |
0.4 | - |
NADPH | pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme E216Q, determined by by measuring oxygen consumption | Nocardia farcinica | |
0.4 | - |
NADPH | pH 7.5, 25°C, cosubstrate L-lysine, wild-type enzyme, determined by by measuring oxygen consumption | Nocardia farcinica | |
1.5 | - |
NADPH | pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme R301A, determined by by measuring oxygen consumption | Nocardia farcinica | |
2.6 | - |
NADPH | pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme E216Q, determined by by measuring oxygen consumption | Nocardia farcinica |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Nocardia farcinica | Q5Z1T5 | - |
- |
Nocardia farcinica IFM 10152 | Q5Z1T5 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-lysine + NADH + H+ + O2 | the enzyme displays a 3fold preference for NADPH over NADH. R301 plays a major role in NADPH selectivity by interacting with the 2'-phosphate of the adenine-ribose moiety of NADPH, while E216 plays a role in L-Lys binding and FAD reduction | Nocardia farcinica | N6-hydroxy-L-lysine + NAD+ + H2O | - |
? | |
L-lysine + NADH + H+ + O2 | the enzyme displays a 3fold preference for NADPH over NADH. R301 plays a major role in NADPH selectivity by interacting with the 2'-phosphate of the adenine-ribose moiety of NADPH, while E216 plays a role in L-Lys binding and FAD reduction | Nocardia farcinica IFM 10152 | N6-hydroxy-L-lysine + NAD+ + H2O | - |
? | |
L-lysine + NADPH + H+ + O2 | the enzyme displays a 3fold preference for NADPH over NADH. R301 plays a major role in NADPH selectivity by interacting with the 2'-phosphate of the adenine-ribose moiety of NADPH, while E216 plays a role in L-Lys binding and FAD reduction | Nocardia farcinica | N6-hydroxy-L-lysine + NADP+ + H2O | - |
? | |
L-lysine + NADPH + H+ + O2 | the enzyme displays a 3fold preference for NADPH over NADH. R301 plays a major role in NADPH selectivity by interacting with the 2'-phosphate of the adenine-ribose moiety of NADPH, while E216 plays a role in L-Lys binding and FAD reduction | Nocardia farcinica IFM 10152 | N6-hydroxy-L-lysine + NADP+ + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
lysine N6-monooxygenase | - |
Nocardia farcinica |
NbtG | - |
Nocardia farcinica |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Nocardia farcinica |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.7 | - |
NADPH | pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme M239R, determined by by measuring oxygen consumption | Nocardia farcinica | |
0.8 | - |
NADPH | pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme R301A, determined by by measuring oxygen consumption | Nocardia farcinica | |
0.98 | - |
NADPH | pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme M239R, determined by by measuring oxygen consumption | Nocardia farcinica | |
1.08 | - |
NADPH | pH 7.5, 25°C, cosubstrate L-lysine, wild-type enzyme, determined by by measuring oxygen consumption | Nocardia farcinica | |
1.29 | - |
NADPH | pH 7.5, 25°C, cosubstrate L-lysine, wild-type enzyme, determined by by measuring oxygen consumption | Nocardia farcinica | |
2.4 | - |
NADPH | pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme E216Q, determined by by measuring oxygen consumption | Nocardia farcinica |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Nocardia farcinica |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | E216 plays a role in L-Lys binding and FAD reduction | Nocardia farcinica | |
NADH | the enzyme displays a 3fold preference for NADPH over NADH. R301 plays a major role in NADPH selectivity by interacting with the 2'-phosphate of the adenine-ribose moiety of NADPH | Nocardia farcinica | |
NADPH | the enzyme displays a 3fold preference for NADPH over NADH. R301 plays a major role in NADPH selectivity by interacting with the 2'-phosphate of the adenine-ribose moiety of NADPH | Nocardia farcinica |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.026 | - |
NADPH | pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme R301A, determined by by measuring oxygen consumption | Nocardia farcinica | |
0.545 | - |
NADPH | pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme R301A, determined by by measuring oxygen consumption | Nocardia farcinica | |
0.94 | - |
NADPH | pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme E216Q, determined by by measuring oxygen consumption | Nocardia farcinica | |
3.3 | - |
NADPH | pH 7.5, 25°C, cosubstrate L-lysine, wild-type enzyme, determined by by measuring oxygen consumption | Nocardia farcinica | |
5.95 | - |
NADPH | pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme E216Q, determined by by measuring oxygen consumption | Nocardia farcinica | |
7.7 | - |
NADPH | pH 7.5, 25°C, cosubstrate L-lysine, wild-type enzyme, determined by by measuring oxygen consumption | Nocardia farcinica | |
8.9 | - |
NADPH | pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme M239R, determined by by measuring oxygen consumption | Nocardia farcinica | |
10.7 | - |
NADPH | pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme M239R, determined by by measuring oxygen consumption | Nocardia farcinica |