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Literature summary for 1.1.98.6 extracted from

  • Andersson, J.; Westman, M.; Sahlin, M.; Sjoberg, B.M.
    Cysteines involved in radical generation and catalysis of class III anaerobic ribonucleotide reductase. A protein engineering study of bacteriophage T4 NrdD (2000), J. Biol. Chem., 275, 19449-19455.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Tequatrovirus T4

Protein Variants

Protein Variants Comment Organism
C260S activity comparable to wild-type, mutant is able to undergo truncation at the site of the glycyl radical when the radical-containing enzyme is exposed to oxygen Tequatrovirus T4
C290S residue participates in the reaction mechanism by forming a transient thiyl radical. Mutant is able to undergo truncation at the site of the glycyl radical when the radical-containing enzyme is exposed to oxygen Tequatrovirus T4
C453S activity comparable to wild-type, mutant is able to undergo truncation at the site of the glycyl radical when the radical-containing enzyme is exposed to oxygen Tequatrovirus T4
C543S residue is essential for formation of the glycyl radical Tequatrovirus T4
C546S residue is essential for formation of the glycyl radical Tequatrovirus T4
C561S residue is essential for formation of the glycyl radical Tequatrovirus T4
C564S residue is essential for formation of the glycyl radical Tequatrovirus T4
C579S mutant is able to undergo truncation at the site of the glycyl radical when the radical-containing enzyme is exposed to oxygen Tequatrovirus T4
C79S residue participates in the actual reduction of the substrate. Mutant is able to undergo truncation at the site of the glycyl radical when the radical-containing enzyme is exposed to oxygen Tequatrovirus T4
G580A oxygen-dependent cleavage is not possible in this mutant since no radical can be formed at Ala580 Tequatrovirus T4

Organism

Organism UniProt Comment Textmining
Tequatrovirus T4 P07071
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