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Literature summary for 1.13.11.6 extracted from

  • Zhang, Y.; Colabroy, K.L.; Begley, T.P.; Ealick, S.E.
    Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: the catalytic mechanism of a complex oxidation involved in NAD biosynthesis (2005), Biochemistry, 44, 7632-7643.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop method Cupriavidus metallidurans

Protein Variants

Protein Variants Comment Organism
E110A kcat/Km is 954fold lower than wild-type enzyme Cupriavidus metallidurans
R47A kcat/Km is 7440fold lower than wild-type enzyme. Mutant enzyme shows substrate inhibition Cupriavidus metallidurans
R99A kcat/Km is 22320fold lower than wild-type enzyme Cupriavidus metallidurans

Inhibitors

Inhibitors Comment Organism Structure
4-Chloro-3-hydroxyanthranilate
-
Cupriavidus metallidurans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0102
-
3-Hydroxyanthranilate pH 7.2, mutant enzyme E110A Cupriavidus metallidurans
0.0224
-
3-Hydroxyanthranilate pH 7.2, wild-type enzyme Cupriavidus metallidurans
0.147
-
3-Hydroxyanthranilate pH 7.2, mutant enzyme R47A Cupriavidus metallidurans
0.872
-
3-Hydroxyanthranilate pH 7.2, mutant enzyme R99A Cupriavidus metallidurans

Metals/Ions

Metals/Ions Comment Organism Structure
Fe each monomer contains two iron binding sites. The catalytic iron is buried deep inside the beta-barrel with His51, Glu57, and His95 serving as ligands. The other iron site forms an FeS4 center close to the solvent surface in which the sulfur atoms are provided by Cys125, Cys128, Cys162, and Cys165. The two iron sites are separated by 24 A Cupriavidus metallidurans

Organism

Organism UniProt Comment Textmining
Cupriavidus metallidurans
-
recombinantly expressed in Escherichia coli
-

Purification (Commentary)

Purification (Comment) Organism
-
Cupriavidus metallidurans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-hydroxyanthranilate + O2
-
Cupriavidus metallidurans 2-amino-3-carboxymuconate semialdehyde
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0046
-
3-Hydroxyanthranilate pH 7.2, mutant enzyme R99A Cupriavidus metallidurans
0.012
-
3-Hydroxyanthranilate pH 7.2, mutant enzyme E110A Cupriavidus metallidurans
0.022
-
3-Hydroxyanthranilate pH 7.2, mutant enzyme R47A Cupriavidus metallidurans
25
-
3-Hydroxyanthranilate pH 7.2, wild-type enzyme Cupriavidus metallidurans