HAAO

3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) is an enzyme encoded by the HAAO gene that catalyzes the chemical reaction

3-hydroxyanthranilate + O2 2-amino-3-carboxymuconate semialdehyde
3-hydroxyanthranilic acid dioxygenase
Identifiers
Aliases3hydroanth_dOaseIPR0103293-hydroxyanthranilate 3,4-dioxygenase3-hydroxyanthranilate oxygenase3-hydroxyanthranilic oxygenase3-hydroxyanthranilate:oxygen 3,4-oxidoreductase (decyclizing)3-hydroxyanthranilic acid oxygenase
External IDsGeneCards:
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human
3-hydroxyanthranilate 3,4-dioxygenase
3-hydroxyanthranilate 3,4-dioxygenase monomer, Human
Identifiers
EC number1.13.11.6
CAS number9029-50-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Thus, the two substrates of this enzyme are 3-hydroxyanthranilate and O2, whereas its product is 2-amino-3-carboxymuconate semialdehyde.

This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2.

The systematic name of this enzyme class is 3-hydroxyanthranilate:oxygen 3,4-oxidoreductase (decyclizing). Other names in common use include 3-hydroxyanthranilate oxygenase, 3-hydroxyanthranilic acid oxygenase, 3-hydroxyanthranilic oxygenase, 3-hydroxyanthranilic acid oxidase and 3HAO. This enzyme participates in tryptophan metabolism. It employs one cofactor, iron.

Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1YFU, 1YFW, 1YFX, 1YFY, 1ZVF, and 2QNK.

References
    • DECKER RH, KANG HH, LEACH FR, HENDERSON LM (1961). "Purification and properties of 3-hydroxyanthranilic acid oxidase". J. Biol. Chem. 236: 3076–82. PMID 13884755.
    • Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 8, Academic Press, New York, 1963, p. 353-371.
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