D-mannitol oxidase
| d-mannitol oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.3.40 | ||||||||
| 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, d-mannitol oxidase (EC 1.1.3.40) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are mannitol and oxygen. Its products are D-mannose and hydrogen peroxide.[1][2][3]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is mannitol:oxygen oxidoreductase (cyclizing). Other names in common use include mannitol oxidase, and D-arabitol oxidase.
References
- ^ Enzyme 1.1.3.40 at KEGG Pathway Database.
- ^ Vorhaben JE, Smith DD Jr, Campbell JW (1986). "Mannitol oxidase: partial purification and characterization of the membrane-bound enzyme from the snail Helix aspersa". Int. J. Biochem. 18 (4): 337–44. doi:10.1016/0020-711X(86)90039-X. PMID 3519307.
- ^ Large AT, Jones CJP, Connock MJ (1993). "The association of mannitol oxidase with a distinct organelle in the digestive gland of the terrestrial slug Arion ater". Protoplasma. 175 (3–4): 93–101. Bibcode:1993Prpls.175...93L. doi:10.1007/BF01385006.