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Literature summary for 1.1.98.6 extracted from

  • Ollagnier, S.; Mulliez, E.; Schmidt, P.P.; Eliasson, R.; Gaillard, J.; Deronzier, C.; Bergman, T.; Graeslund, A.; Reichard, P.; Fontecave, M.
    Activation of the anaerobic ribonucleotide reductase from Escherichia coli. The essential role of the iron-sulfur center for S-adenosylmethionine reduction (1997), J. Biol. Chem., 272, 24216-24223.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine S-adenosyl-L-methionine is directly reduced by the Fe-S center of the small subunits during the activation of the enzyme, resulting in methionine and glycyl radical formation. S-adenosyl-L-methionine binds to the small subunits with a Kd of 10 microM and a 1:1 stoichiometry. Dithiothreitol triggers the cleavage of S-adenosyl-L-methionine, leading glycyl radical formation. 3 methionines are formed per mol of protein Escherichia coli
[4Fe-4S]-center S-adenosyl-L-methionine is directly reduced by the Fe-S center of the small subunits during the activation of the enzyme Escherichia coli