L-ascorbate peroxidase
In enzymology, a L-ascorbate peroxidase (EC 1.11.1.11) is an enzyme that catalyzes the chemical reaction
- L-ascorbate + H2O2 dehydroascorbate + 2 H2O
| L-ascorbate peroxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.11.1.11 | ||||||||
| CAS number | 72906-87-7 | ||||||||
| 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 | ||||||||
| |||||||||
Thus, the two substrates of this enzyme are L-ascorbate and H2O2, whereas its two products are dehydroascorbate and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a peroxide as acceptor (peroxidases). The systematic name of this enzyme class is L-ascorbate:hydrogen-peroxide oxidoreductase. Other names in common use include L-ascorbic acid peroxidase, L-ascorbic acid-specific peroxidase, ascorbate peroxidase, and ascorbic acid peroxidase. This enzyme participates in ascorbate and aldarate metabolism.
Structural studies
As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1APX, 1IYN, 1OAF, 1OAG, 1V0H, 2CL4, 2GGN, 2GHC, 2GHD, 2GHE, 2GHH, and 2GHK.
References
- Shigeoka S, Nakano Y, Kitaoka S (1980). "Purification and some properties of L-ascorbic-acid-specific peroxidase in Euglena gracilis Z". Arch. Biochem. Biophys. 201 (1): 121–7. doi:10.1016/0003-9861(80)90495-6. PMID 6772104.
- Shigeoka S, Nakano Y, Kitaoka S (1980). "Metabolism of hydrogen peroxide in Euglena gracilis Z by L-ascorbic acid peroxidase". Biochem. J. 186 (1): 377–80. PMC 1161541. PMID 6768357.