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Literature summary for 1.1.98.6 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.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Tequatrovirus T4

Protein Variants

Protein Variants Comment Organism
C290S mutation in conserved residua, less than 10% of wild-type activity Tequatrovirus T4

Organism

Organism UniProt Comment Textmining
Tequatrovirus T4 P07071
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
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Synonyms

Synonyms Comment Organism
nrdD
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Tequatrovirus T4