Aryl formamidase
| Aryl formamidase | ||
|---|---|---|
| Properties of human protein | ||
| Mass / length primary structure | 308 amino acids | |
| Identifier | ||
| Gene name | AFMID | |
| External IDs | ||
| Enzyme classification | ||
| EC, category | 3.5.1.9 , hydrolase | |
| Response type | Spin-off from formate | |
| Substrate | N-formylkynurenine + H 2 O | |
| Products | Kynurenine + formate | |
| Occurrence | ||
| Homology family | Aryl formamidase | |
| Parent taxon | Euteleostomi | |
In the arylformamidase (KF) is the enzyme that the second part of step, decomposition of the amino acid tryptophan , namely the elimination of formate of N-formylkynurenine catalyzed . The enzyme is found in vertebrates . In humans it is produced in all types of tissue.
Mice without KF show problems with the kidneys and the immune system, but can partially break down N-formylkynurenine. This means that there is likely another enzyme catalyzing this reaction.
The AFMID - gene coding for the arylformamidase encoded , is the rare example of a gene whose expression inversely with the acetylation of histone in the promoter correlated.
Catalyzed reaction
+ H 2 O + HCOO - 
Formic acid is split off from N -formyl- L- kynurenine by hydrolysis and L- kynurenine is formed.
Individual evidence
- ↑ UniProt Q63HM1
- ↑ BioGPS entry
- ↑ Dobrovolsky VN, Bowyer JF, Pabarcus MK, et al : Effect of arylformamidase (kynurenine formamidase) gene inactivation in mice on enzymatic activity, kynurenine pathway metabolites and phenotype . In: Biochim. Biophys. Acta . 1724, No. 1-2, June 2005, pp. 163-72. doi : 10.1016 / j.bbagen.2005.03.010 . PMID 15866519 .
- ↑ Schuettengruber B, Doetzlhofer A, Kroboth K, Wintersberger E, Seiser C: Alternate activation of two divergently transcribed mouse genes from a bidirectional promoter is linked to changes in histone modification . In: J. Biol. Chem. . 278, No. 3, January 2003, pp. 1784-93. doi : 10.1074 / jbc.M204843200 . PMID 12411446 .
