Biology:L-ascorbate oxidase
| L-ascorbate oxidase | |||||||||
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| Identifiers | |||||||||
| EC number | 1.10.3.3 | ||||||||
| CAS number | 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 | ||||||||
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L-ascorbate oxidase (EC 1.10.3.3) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are L-ascorbic acid (vitamin C) and oxygen. Its products are dehydroascorbic acid and water.[1][2][3]
Function
This enzyme belongs to the family of oxidoreductases, specifically those acting on diphenols and related substances as donor with oxygen as acceptor. It participates in ascorbate metabolism. It employs one cofactor, copper. An X-ray structure has been published.[4]
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
- ↑ Enzyme 1.10.3.3 at KEGG Pathway Database.
- ↑ "Ascorbate oxidase.". Copper Proteins and Copper Enzymes. Boca Raton: CRC Press. February 1984. pp. 101–118. doi:10.1201/9781351070898. ISBN 978-1-351-07089-8.
- ↑ The Enzymes. 8 (2nd ed.). New York: Academic Press. 1963. pp. 297–311.
- ↑ Messerschmidt, Albrecht; Ladenstein, Rudolf; Huber, Robert; Bolognesi, Martino; Avigliano, Luciana; Petruzzelli, Raffaele; Rossi, Antonello; Finazzi-Agró, Alessandro (1992). "Refined crystal structure of ascorbate oxidase at 1.9 Å resolution". Journal of Molecular Biology 224 (1): 179–205. doi:10.1016/0022-2836(92)90583-6. PMID 1548698.
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