| EC Tree |
| 1. Oxidoreductases |
| 1.10 Acting on diphenols and related substances as donors |
| 1.10.2 With a cytochrome as acceptor |
| ID: | 1.10.2.1 |
|---|---|
| Description: | L-ascorbate--cytochrome-b5 reductase. |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 1.10.2.1 |
| BRENDA Enzyme Link: | BRENDA 1.10.2.1 |
| KEGG Enzyme Link: | KEGG1.10.2.1 |
| BioCyc Enzyme Link: | BioCyc 1.10.2.1 |
| ExPASy Enzyme Link: | ExPASy1.10.2.1 |
| EC2PDB Enzyme Link: | EC2PDB 1.10.2.1 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.10.2.1 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.10.2.1 |
| IntEnz Enzyme Link: | IntEnz 1.10.2.1 |
| MEDLINE Enzyme Link: | MEDLINE 1.10.2.1 |
| RHEA:18677 | [Fe(III)-cytochrome b5] + L-ascorbate = [Fe(II)-cytochrome b5] + H(+) + monodehydro-L-ascorbate radical |
| RULE(radius=1) | [Fe+3;H0:1]>>[Fe+2;H0:1] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| [Kinetic studies on an ascorbate: ferricytochrome b5 oxidoreductase (EC 1.1.2.?)]. | Everling FB, Weis W, Staudinger H | 1969 Dec | 5363650 |