L-ascorbate—cytochrome-b5 reductase
| L-ascorbate—cytochrome-b5 reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.10.2.1 | ||||||||
| CAS number | 37237-57-3 | ||||||||
| 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 / EGO | ||||||||
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In enzymology, a L-ascorbate—cytochrome-b5 reductase (EC 1.10.2.1) is an enzyme that catalyzes the chemical reaction
- L-ascorbate + ferricytochrome b5 monodehydroascorbate + ferrocytochrome b5 + H+
 
Thus, the two substrates of this enzyme are L-ascorbate and ferricytochrome b5, whereas its 3 products are monodehydroascorbate, ferrocytochrome b5, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on diphenols and related substances as donor with a cytochrome as acceptor. The systematic name of this enzyme class is L-ascorbate:ferricytochrome-b5 oxidoreductase. This enzyme is also called ascorbate-cytochrome b5 reductase.
References
- Everling FB, Weis W, Staudinger H (1969). "[Kinetic studies on an ascorbate: ferricytochrome b5 oxidoreductase (EC 1.1.2.?)]". Hoppe. Seylers. Z. Physiol. Chem. 350 (12): 1485–92. PMID 5363650.
 
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