View source for HAAO

{{Short description|Enzyme}}
{{Infobox gene}}
{{infobox enzyme
| Name       = 3-hydroxyanthranilate 3,4-dioxygenase
| EC_number  = 1.13.11.6
| CAS_number = 9029-50-9
| GO_code    = 0000334
| image      = 5tk5.jpg
| width      = 270
| caption    = 3-hydroxyanthranilate 3,4-dioxygenase monomer, Human
}}
'''3-hydroxyanthranilate 3,4-dioxygenase''' ({{EC number|1.13.11.6}}) is an [[enzyme]] encoded by the '''''HAAO''''' gene that [[catalysis|catalyzes]] the [[chemical reaction]]

:[[3-hydroxyanthranilate]] + [[Oxygen|O<sub>2</sub>]] <math>\rightleftharpoons</math> [[2-amino-3-carboxymuconate semialdehyde]]

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are 3-hydroxyanthranilate and O<sub>2</sub>, whereas its [[product (chemistry)|product]] is 2-amino-3-carboxymuconate semialdehyde.

This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on single donors with O<sub>2</sub> as oxidant and incorporation of two atoms of oxygen into the substrate ([[oxygenases]]). The oxygen incorporated need not be derived from O<sub>2</sub>.

The [[List of enzymes|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 (biochemistry)|cofactor]], [[iron]].

==Structural studies==

As of late 2007, 6 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1YFU}}, {{PDB link|1YFW}}, {{PDB link|1YFX}}, {{PDB link|1YFY}}, {{PDB link|1ZVF}}, and {{PDB link|2QNK}}.h

==References==
{{reflist|1}}
* {{cite journal | vauthors = DECKER RH, KANG HH, LEACH FR, HENDERSON LM | date = 1961 | title = Purification and properties of 3-hydroxyanthranilic acid oxidase | journal = J. Biol. Chem.  | volume = 236 | issue = 11 | pages = 3076–82  | doi = 10.1016/S0021-9258(19)76432-1 | pmid = 13884755 | doi-access = free }}
* Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 8, Academic Press, New York, 1963, p.&nbsp;353-371.

{{Monooxygenases}}
{{Enzymes}}
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[[Category:EC 1.13.11]]
[[Category:Iron enzymes]]
[[Category:Enzymes of known structure]]