Literature summary extracted from
Olcott, M.C.; Andersson, J.; Sjoeberg, B.M.
Localization and characterization of two nucleotide-binding sites on the anaerobic ribonucleotide reductase from bacteriophage T4 (1998), J. Biol. Chem., 273, 24853-24860.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.1.98.6 |
expression in Escherichia coli |
Tequatrovirus T4 |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
1.1.98.6 |
C290S |
mutation in conserved residua, less than 10% of wild-type activity |
Tequatrovirus T4 |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.1.98.6 |
Tequatrovirus T4 |
P07071 |
- |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.1.98.6 |
additional information |
the enzyme displays two nucleotide-binding sites. One site exhibits half-maximal saturation at approximately 5 mM 8-azidoadenosine 5'-triphosphate, whereas the other site requires 45 microM. The higher affinity site corresponds to residues 289-291 and the other site to the region to residues 147-160. Photoinsertion of 8-azidoadenosine 5'-triphosphate into the site corresponding to residues 147-160 is almost completely abolished when 100 mM dATP, dGTP, or dTTP is included in the photolabeling reaction mixture, whereas 100 mM ATP, GTP, CTP, or dCTP have virtually no effect |
Tequatrovirus T4 |
? |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.1.98.6 |
nrdD |
- |
Tequatrovirus T4 |