Ascorbate peroxidase
| L-ascorbate peroxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Structure of ascorbate peroxidase in complex with ascorbate (in blue); a histidine ligand (in red) coordinates to the iron of the heme group (also in red). Image taken from PDB 1OAF and created using Pymol | |||||||||
| Identifiers | |||||||||
| EC no. | 1.11.1.11 | ||||||||
| CAS no. | 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 | ||||||||
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Ascorbate peroxidase (or L-ascorbate peroxidase, APX or APEX) (EC 1.11.1.11) is an enzyme that catalyzes the overall chemical reaction:
It is a member of the family of heme-containing peroxidases. Heme peroxidases catalyse the hydrogen peroxide-dependent oxidation of a wide range of different, usually organic, substrates in biology.
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 the ascorbate and aldarate metabolism. APXs are important in cellular antioxidant networks in photosynthetic organisms; they are the primary component of the ascorbate-glutathione cycle and are important for peroxide scavenging and redox signaling.