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Literature summary for 1.17.4.1 extracted from

  • Yun, D.; Krebs, C.; Gupta, G.P.; Iwig, D.F.; Huynh, B.H.; Bollinger, J.M., Jr.
    Facile electron transfer during formation of cluster x and kinetic competence of x for tyrosyl radical production in protein R2 of ribonucleotide reductase from mouse (2002), Biochemistry, 41, 981-990.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and Y177F mutant subunit R2 in Escherichia coli Mus musculus

Protein Variants

Protein Variants Comment Organism
Y177F tyrosyl residue involved in radical formation Mus musculus

Metals/Ions

Metals/Ions Comment Organism Structure
additional information the essential metallo-cofactor is a micro-oxo-micro-carboxylato-diiron cluster adjacent to a stable tyrosyl radical Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
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Reaction

Reaction Comment Organism Reaction ID
2'-deoxyribonucleoside 5'-diphosphate + thioredoxin disulfide + H2O = ribonucleoside 5'-diphosphate + thioredoxin kinetics and mechanism of formation of the tyrosyl radical and micro-oxo-diiron cluster in the R2 subunit Mus musculus