ENZYME entry: EC 1.1.98.6
| Accepted Name |
|---|
| Ribonucleoside-triphosphate reductase (formate).
|
| Alternative Name(s) |
|---|
| Anaerobic ribonucleoside-triphosphate reductase. |
| Reaction catalysed |
|---|
| Ribonucleoside 5'-triphosphate + formate <=> 2'-deoxyribonucleoside 5'-triphosphate + CO(2) + H(2)O |
| Comment(s) |
|---|
- The enzyme, which is expressed in the bacterium Escherichia coli
during anaerobic growth, contains an iron sulfur center.
- The active form of the enzyme contains an oxygen-sensitive glycyl
(1-amino-2-oxoethan-1-yl) radical that is generated by the activating
enzyme NrdG via chemistry involving S-adenosylmethionine (SAM) and a
[4Fe-4S] cluster.
- The glycyl radical is involved in generation of a transient thiyl
(sulfanyl) radical on a cysteine residue, which attacks the
substrate, forming a ribonucleotide 3'-radical, followed by water
loss to form a ketyl (alpha-oxoalkyl) radical.
- The ketyl radical gains an electron from a cysteine residue and a
proton from formic acid, forming 3'-keto-deoxyribonucleotide and
generating a thiosulfuranyl (1-lambda(4)-disulfan-1-yl) radical
bridge between methionine and cysteine residues.
- Oxidation of formate by the thiosulfuranyl radical results in the
release of CO(2) and regeneration of the thiyl radical.
- Cf. EC 1.17.4.1 and EC 1.17.4.2.
|
| Cross-references |
|---|
| BRENDA | 1.1.98.6 |
| EC2PDB | 1.1.98.6 |
| ExplorEnz | 1.1.98.6 |
| PRIAM enzyme-specific profiles | 1.1.98.6 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.1.98.6 |
| IUBMB Enzyme Nomenclature | 1.1.98.6 |
| IntEnz | 1.1.98.6 |
| MEDLINE | Find literature relating to 1.1.98.6 |
| MetaCyc | 1.1.98.6 |
| UniProtKB/Swiss-Prot |
|
View entry in original ENZYME format
View entry in raw text format (no links)
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 1.1.98.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-