EC Number   |
General Information |
Reference |
|---|
    1.13.11.6 | evolution |
HAD belongs to the class of nonheme iron(II) enzymes and shares functional similarity with extradiol-cleaving catechol dioxygenases |
723950 |
| 1.13.11.6 | metabolism |
3-hydroxyanthranilate 3,4-dioxygenase (3HAO) is an enzyme in the microglial branch of the kynurenine pathway of tryptophan degradation |
741516 |
| 1.13.11.6 | more |
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 |
743276 |
| 1.13.11.6 | more |
oxidative CC bond cleavage of 2-amino-4-tert-butylphenolate on complex nonheme iron(II) complex, [(6-Me3-TPA)FeII(4-tBu-HAP)](ClO4) is mimicking the enzyme function. The iron(II)-aminophenolate complex reacts with molecular oxygen in acetonitrile under ambient conditions, overview |
723950 |
| 1.13.11.6 | more |
residue Met35 is involved in interactions with substrates and inhibitors |
741516 |
| 1.13.11.6 | physiological function |
enzyme 3HAO is a non-heme iron-containing, ring-cleaving extradiol dioxygenase that catalyzes the addition of both atoms of O2 to the kynurenine pathway metabolite 3-hydroxyanthranilic acid (3-HANA) to form quinolinic acid. Quinolinic acid is a highly potent excitotoxin that is implicated in a number of neurodegenerative conditions |
741516 |
| 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 |
743276 |
| 1.13.11.6 | physiological function |
the enzyme catalyzes the degradation of 3-hydroxyanthranilate to quinolinate in the presence of dioxygen |
723950 |
