HAAO
| 3-hydroxyanthranilic acid dioxygenase | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | 3hydroanth_dOaseIPR0103293-hydroxyanthranilate 3,4-dioxygenase3-hydroxyanthranilate oxygenase3-hydroxyanthranilic oxygenase3-hydroxyanthranilate:oxygen 3,4-oxidoreductase (decyclizing)3-hydroxyanthranilic acid oxygenase | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | GeneCards: [1]; OMA:- orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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| Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| 3-hydroxyanthranilate 3,4-dioxygenase | |||||||||
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3-hydroxyanthranilate 3,4-dioxygenase monomer, Human | |||||||||
| Identifiers | |||||||||
| EC no. | 1.13.11.6 | ||||||||
| CAS no. | 9029-50-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) is an enzyme encoded by the HAAO gene that catalyzes the chemical reaction
The two substrates of this enzyme are 3-hydroxyanthranilic acid and oxygen. Its product is 2-amino-3-carboxymuconic semialdehyde.[1][2][3][4]
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.h
References
- ^ Enzyme 1.13.11.6 at KEGG Pathway Database.
- ^ Decker, R.H.; Kang, H.H.; Leach, Franklin R.; Henderson, L.M. (1961). "Purification and Properties of 3-Hydroxyanthranilic Acid Oxidase". Journal of Biological Chemistry. 236 (11): 3076–3082. doi:10.1016/S0021-9258(19)76432-1.
- ^ Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 8, Academic Press, New York, 1963, p. 353-371.
- ^ Davis, Ian; Yang, Yu; Wherritt, Daniel; Liu, Aimin (2018). "Reassignment of the human aldehyde dehydrogenase ALDH8A1 (ALDH12) to the kynurenine pathway in tryptophan catabolism". Journal of Biological Chemistry. 293 (25): 9594–9603. doi:10.1074/jbc.RA118.003320. PMC 6016481. PMID 29703752.