Any feedback?
Literature summary for 1.17.4.1 extracted from
- Ribonucleotide reductase - a radical enzyme (1983), Science, 221, 514-519.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Iron | iron center stabilizes tyrosyl radical, distance between the iron center and the tyrosyl radical is estimated to be 6-9.0 A | Escherichia coli |  |
| Iron | iron binds directly to the enzyme structure and not via sulfur | Escherichia coli | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 2'-deoxyribonucleoside 5'-diphosphate + thioredoxin disulfide + H2O = ribonucleoside 5'-diphosphate + thioredoxin | proposed mechanism | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ribonucleoside diphosphate + reduced thioredoxin | - |
Escherichia coli | 2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O | - |
ir | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | tyrosyl radical is stabilized by an iron center | Escherichia coli |
| More | the active form of B2 subunit contains a tyrosyl radical essential for activity | Escherichia coli |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
