L-ascorbate peroxidase

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In enzymology, a L-ascorbate peroxidase (EC 1.11.1.11) is an enzyme that catalyzes the chemical reaction

L-ascorbate + H₂O₂ $\rightleftharpoons$ dehydroascorbate + 2 H₂O

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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] 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.

[edit] References

IUBMB entry for 1.11.1.11
BRENDA references for 1.11.1.11 (Recommended.)
PubMed references for 1.11.1.11
PubMed Central references for 1.11.1.11
Google Scholar references for 1.11.1.11
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: 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: 377–80. PMID 6768357.