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Literature summary 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)

EC Number Crystallization (Comment) Organism
1.13.11.6 hanging drop method Cupriavidus metallidurans

Protein Variants

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.13.11.6 4-Chloro-3-hydroxyanthranilate
-
 Cupriavidus metallidurans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.6 0.0102
-
 3-Hydroxyanthranilate pH 7.2, mutant enzyme E110A Cupriavidus metallidurans
1.13.11.6 0.0224
-
 3-Hydroxyanthranilate pH 7.2, wild-type enzyme Cupriavidus metallidurans
1.13.11.6 0.147
-
 3-Hydroxyanthranilate pH 7.2, mutant enzyme R47A Cupriavidus metallidurans
1.13.11.6 0.872
-
 3-Hydroxyanthranilate pH 7.2, mutant enzyme R99A Cupriavidus metallidurans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.6 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

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.11.6
-
 Cupriavidus metallidurans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.6 3-hydroxyanthranilate + O2
-
 Cupriavidus metallidurans 2-amino-3-carboxymuconate semialdehyde
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.13.11.6 0.0046
-
 3-Hydroxyanthranilate pH 7.2, mutant enzyme R99A Cupriavidus metallidurans
1.13.11.6 0.012
-
 3-Hydroxyanthranilate pH 7.2, mutant enzyme E110A Cupriavidus metallidurans
1.13.11.6 0.022
-
 3-Hydroxyanthranilate pH 7.2, mutant enzyme R47A Cupriavidus metallidurans
1.13.11.6 25
-
 3-Hydroxyanthranilate pH 7.2, wild-type enzyme Cupriavidus metallidurans