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Literature summary for 1.13.11.6 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
Search for more literature for 1.13.11.6

Application

Application Comment Organism
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

Protein Variants Comment Organism
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
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
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

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens P46952
-
-

Substrates and Products (Substrate)

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

General Information

General Information Comment Organism
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
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