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Literature summary for 1.14.13.59 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
Search for more literature for 1.14.13.59

Cloned(Commentary)

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

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

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

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

Synonyms Comment Organism
IucD
-
 Escherichia coli
lysine: N6-hydroxylase
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at Escherichia coli

Cofactor

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