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// Workers AI · dad joke modeWhat did HAAO say to its friend? Ha ha oh.

From Wikipedia, the free encyclopedia

{

HAAO
Identifiers
AliasesHAAO, Haao, 0610007K21Rik, 0610012J07Rik, 3-HAO, 3-HAOxase, 3HAO, HAO, 3-hydroxyanthranilate 3,4-dioxygenase, VCRL1, h3HAO
External IDsOMIM: 604521; MGI: 1349444; HomoloGene: 8148; GeneCards: HAAO; OMA:HAAO - orthologs
Available structures
PDBOrtholog search: PDBe RCSB
Enzyme activity
EC #BRENDAExPASyKEGGMetaCyc
1.13.11.6
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_012205

NM_025325

RefSeq (protein)

NP_036337

NP_079601

Location (UCSC)Chr 2: 42.77 – 42.79 MbChr 17: 84.14 – 84.16 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
3-hydroxyanthranilate 3,4-dioxygenase
3-hydroxyanthranilate 3,4-dioxygenase monomer, Human
Identifiers
EC no.1.13.11.6
CAS no.9029-50-9
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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

 
O2
 
Rightward reaction arrow with minor substrate(s) from top left
 
 
 

The two substrates of this enzyme are 3-hydroxyanthranilic acid and oxygen. Its product is 2-amino-3-carboxymuconic semialdehyde.[5][6][7][8]

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

[edit]

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

References

[edit]
  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000162882 Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000000673 Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Enzyme 1.13.11.6 at KEGG Pathway Database.
  6. Decker R, Kang H, Leach FR, Henderson L (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.
  7. Boyer PD, Lardy H, Myrback K, eds. (1963). The Enzymes. Vol. 8 (2nd ed.). New York: Academic Press. pp. 353–371.
  8. Davis I, Yang Y, Wherritt D, Liu A (June 2018). "Reassignment of the human aldehyde dehydrogenase ALDH8A1 (ALDH12) to the kynurenine pathway in tryptophan catabolism". The Journal of Biological Chemistry. 293 (25): 9594–9603. doi:10.1074/jbc.RA118.003320. PMC 6016481. PMID 29703752.