Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutants in strain DH5alpha | Escherichia coli |
General Stability | Organism |
---|---|
enzyme is sensitive to deleterious action of proteases, FAD and ADP protect, while NADPH protects only partially, and L-lysine and L-norleucine are ineffective in protecting the enzyme | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | enzyme is sensitive to deleterious action of endoproteases trypsin, carboxypeptidase Y, and chymotrypsin, FAD and ADP protect, proteolysis of a C-terminal segment results in loss of enzyme activity | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-lysine + NADPH + O2 | - |
Escherichia coli | N6-hydroxy-L-lysine + NADP+ + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | with time the enzyme aggregates to polytetrameric forms, which is reversible by thiols, the C-terminal segment is important for activity and conformational stability | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
IucD | - |
Escherichia coli |
lysine: N6-hydroxylase | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.2 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | required for activity | Escherichia coli | |
NADPH | required for activity | Escherichia coli |