3-hydroxyanthranilate-3,4-dioxygenase
| 3-hydroxyanthranilate-3,4-dioxygenase | ||
|---|---|---|
| Properties of human protein | ||
| Mass / length primary structure | 286 amino acids | |
| Secondary to quaternary structure | Monomer | |
| Cofactor | Fe 2+ | |
| Identifier | ||
| Gene name | HAAO | |
| External IDs | ||
| Enzyme classification | ||
| EC, category | 1.13.11.6 , dioxygenase | |
| Response type | Addition of two oxygen atoms | |
| Substrate | 3-hydroxyanthranilate + O 2 | |
| Products | 2-Amino-3-carboxymuconate semialdehyde | |
| Occurrence | ||
| Parent taxon | Bacteria, fungi, animals | |
3-hydroxyanthranilate-3,4-dioxygenase (3HAO) ( gene : HAAO ) is the name of the enzyme that oxidizes 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde . This reaction step is part of the degradation - pathway of the amino acid tryptophan , the reaction product is also raw material for the biosynthesis of nicotinic acid and NAD . 3HAO is found in many bacteria , fungi and animals. In humans, it is mainly produced in the liver .
Inhibition of 3HAO with 4-chloro-3-hydroxyanthranilate reduced the accumulation of quinolinate in mice with fresh spinal cord injuries and improved the neurological symptoms.
Catalyzed reaction
+ O 2 + H 2 O
3-Hydroxyanthranilate is oxidized to a semialdehyde which spontaneously rearranges to quinolinate .
Individual evidence
- ↑ UniProt P46952
- ↑ BioGPS entry
- ↑ Yates JR, Heyes MP, Blight AR: 4-chloro-3-hydroxyanthranilate reduces local quinolinic acid synthesis, improves functional recovery, and preserves white matter after spinal cord injury . In: J. Neurotrauma . 23, No. 6, June 2006, pp. 866-81. doi : 10.1089 / new 2006.23.866 . PMID 16774472 .
Web links
Wikibooks: Biochemistry and Pathobiochemistry: Tryptophan Metabolism - Learning and Teaching Materials
Wikibooks: Biochemistry and Pathobiochemistry: Nicotinate and Nicotinamide Metabolism - Learning and Teaching Materials