EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.13.11.6 | Fe2+ | required, the active site of HAD contains an iron(II) center that is coordinated by the 2-His-1-Glu facial triad | Pseudomonas oleovorans |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.11.6 | 3-hydroxyanthranilate + O2 | Pseudomonas oleovorans | - |
2-amino-3-carboxymuconate semialdehyde | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.13.11.6 | Pseudomonas oleovorans | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.13.11.6 | 3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde | reaction mechanism, overview | Pseudomonas oleovorans |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.11.6 | 3-hydroxyanthranilate + O2 | - |
Pseudomonas oleovorans | 2-amino-3-carboxymuconate semialdehyde | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.13.11.6 | HAD | - |
Pseudomonas oleovorans |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.13.11.6 | evolution | HAD belongs to the class of nonheme iron(II) enzymes and shares functional similarity with extradiol-cleaving catechol dioxygenases | Pseudomonas oleovorans |
1.13.11.6 | additional information | 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 | Pseudomonas oleovorans |
1.13.11.6 | physiological function | the enzyme catalyzes the degradation of 3-hydroxyanthranilate to quinolinate in the presence of dioxygen | Pseudomonas oleovorans |