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Literature summary extracted from

  • Brkic, H.; Kovacevic, B.; Tomic, S.
    Human 3-hydroxyanthranilate 3,4-dioxygenase dynamics and reaction, a multilevel computational study (2015), Mol. Biosyst., 11, 898-907 .
    View publication on PubMed

Application

EC Number Application Comment Organism
1.13.11.6 drug development the enzyme is a a potential target in treating numerous disorders related to the concentration of quinolinic acid, the kynurenine pathway product Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.6 Q105A site-directed mutagenesis, the mutation affects the enzyme activity, the protein structure, particularly the active site architecture and the metal ion environment, and the substrate binding Homo sapiens
1.13.11.6 R43A site-directed mutagenesis, the mutation affects the enzyme activity, the protein structure, particularly the active site architecture and the metal ion environment, and the substrate binding Homo sapiens
1.13.11.6 R95A site-directed mutagenesis, the mutation affects the enzyme activity, the protein structure, particularly the active site architecture and the metal ion environment, and the substrate binding Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.6 Fe2+ a non-heme iron-containing enzyme Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.6 3-hydroxyanthranilate + O2 Homo sapiens
-
 2-amino-3-carboxymuconate semialdehyde
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.6 Homo sapiens P46952
-
-

Substrates and Products (Substrate)

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

General Information

EC Number General Information Comment Organism
1.13.11.6 additional information enzyme molecular modeling, the water population of the active site, and the protein flexibility as well as the amino acid residues interaction networks are relevant for the enzyme activity, hybrid quantum-mechanics/molecular-mechanics (QM/MM) calculations Homo sapiens
1.13.11.6 physiological function the enzyme catalyses the cleavage of the benzene ring of 3-hydroxyanthranilic acid (3-Ohaa), an intermediate in the kynurenine pathway Homo sapiens