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Literature summary for 1.14.13.59 extracted from

  • Marrone, L.; Beecroft, M.; Viswanatha, T.
    Lysine:N6-hydroxylase: cofactor interactions (1996), Bioorg. Chem., 24, 304-317.
No PubMed abstract available

Protein Variants

Protein Variants Comment Organism
C51A rlucD activity of the genetically engineered enzyme forms C51A rIucD, C51A/C158A eIucD is 1.5times that of the parent rIucD. The activity of C158A rIucD is similar to that of the parent enzyme form Escherichia coli
C51A/C158A rlucD activity of the genetically engineered enzyme forms C51A rIucD, C51A/C158A eIucD is 1.5times that of the parent rIucD. The activity of C158A rIucD is similar to that of the parent enzyme form Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Cl- above 600 mM, enzyme exists in a reversible inactive conformation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.238
-
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FAD requires FAD Escherichia coli
additional information cofactor interactions Escherichia coli
NADPH required Escherichia coli