| L-ascorbate oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifiers | |||||||||
| EC no. | 1.10.3.3 | ||||||||
| CAS no. | 9029-44-1 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a L-ascorbate oxidase (EC 1.10.3.3) is an enzyme that catalyzes the chemical reaction
- 2 L-ascorbate + O2 2 dehydroascorbate + 2 H2O
Thus, the two substrates of this enzyme are L-ascorbate and O2, whereas its two products are dehydroascorbate and H2O.[1]
Function
This enzyme belongs to the family of oxidoreductases, specifically those acting on diphenols and related substances as donor with oxygen as acceptor. This enzyme participates in ascorbate metabolism. It employs one cofactor, copper.
Nomenclature
The systematic name of this enzyme class is L-ascorbate:oxygen oxidoreductase. Other names in common use include ascorbase, ascorbic acid oxidase, ascorbate oxidase, ascorbic oxidase, ascorbate dehydrogenase, L-ascorbic acid oxidase, AAO, L-ascorbate:O2 oxidoreductase, and AA oxidase.
References
- ↑ Mondovì B, Avigliano L (February 1984). "Ascorbate oxidase.". In Lontie R (ed.). Copper Proteins and Copper Enzymes. Boca Raton: CRC Press. pp. 101–118. doi:10.1201/9781351070898. ISBN 978-1-351-07089-8.
Further reading
- Boyer PD, Lardy H, Myrback K, eds. (1963). The Enzymes. Vol. 8 (2nd ed.). New York: Academic Press. pp. 297–311.
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