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Literature summary for 1.11.1.16 extracted from

  • Pogni, R.; Baratto, M.C.; Giansanti, S.; Teutloff, C.; Verdin, J.; Valderrama, B.; Lendzian, F.; Lubitz, W.; Vazquez-Duhalt, R.; Basosi, R.
    Tryptophan-based radical in the catalytic mechanism of versatile peroxidase from Bjerkandera adusta (2005), Biochemistry, 44, 4267-4274.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Bjerkandera adusta
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-
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Reaction

Reaction Comment Organism Reaction ID
1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O study of reaction of H2O2 with the enzyme in the absence of substrate suggests an amino acid radical in moderate distance from ferryl heme. A tryptophan radical is formed during the catalytic mechanism Bjerkandera adusta