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Radical formation on a conserved tyrosine residue is crucial for DyP activity
Eric Strittmatter1, Sabrina Wachter, Christiane Liers
1Institute of Organic Chemistry, Albert-Ludwigs-University, Albertstrasse 21, 79104 Freiburg, Germany.
Abstract:
Dye-decolorizing peroxidases (DyPs) are able to cleave bulky anthraquinone dyes. The recently published crystal structure of AauDyPI reveals that a direct oxidation in the distal heme cavity can be excluded for most DyP substrates. It is shown that a surface-exposed tyrosine residue acts as a substrate interaction site for bulky substrates. This amino acid is conserved in eucaryotic DyPs but is missing in the structurally related chlorite dismutases (Clds). Dye-decolorizing peroxidases of procaryotic origin equally possess a conserved tyrosine in the same region of the polypeptide albeit not at the homologous position.
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