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Literature summary for extracted from

  • Dick, S.; Marrone, L.; Duewel, H.; Beecroft, M.; McCourt, J.; Viswanatha, T.
    Lysine: N6-hydroxylase: stability and interaction with ligands (1999), J. Protein Chem., 18, 893-903.
    View publication on PubMed


Cloned (Comment) Organism
expression of wild-type and mutants in strain DH5alpha Escherichia coli

General Stability

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 and Products (Substrate)

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
Escherichia coli
lysine: N6-hydroxylase
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
assay at Escherichia coli


Cofactor Comment Organism Structure
FAD required for activity Escherichia coli
NADPH required for activity Escherichia coli