Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Mycolicibacterium smegmatis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.2 | 1 | L-lysine | pH 7.5, 25°C | Mycolicibacterium smegmatis | |
1.1 | - |
NADH | pH 7.5, 25°C | Mycolicibacterium smegmatis | |
2.4 | - |
NADPH | pH 7.5, 25°C | Mycolicibacterium smegmatis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycolicibacterium smegmatis | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-lysine + NADH + H+ + O2 | - |
Mycolicibacterium smegmatis | N6-hydroxy-L-lysine + NAD+ + H2O | - |
? | |
L-lysine + NADPH + H+ + O2 | - |
Mycolicibacterium smegmatis | N6-hydroxy-L-lysine + NADP+ + H2O | - |
? | |
additional information | enzyme functions as an oxidase when the activity of MbsG is measured by monitoring oxygen consumption in the absence of L-lysine, oxidizing NADH and NADPH with kcat values of 59 and 49 per min, respectively. Under these conditions, both hydrogen peroxide and superoxide are produced | Mycolicibacterium smegmatis | ? | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.08 | - |
L-lysine | pH 7.5, 25°C | Mycolicibacterium smegmatis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | tigtly bound cofactor | Mycolicibacterium smegmatis | |
NADH | - |
Mycolicibacterium smegmatis | |
NADPH | - |
Mycolicibacterium smegmatis |