title: Radical formation on a conserved tyrosine residue is crucial for DyP activity.
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.
authors.affiliation: Institute of Organic Chemistry, Albert-Ludwigs-University, Albertstrasse 21, 79104 Freiburg, Germany.
authors.forename: Eric
authors.initials: E
authors.lastname: Strittmatter
authors.forename: Sabrina
authors.initials: S
authors.lastname: Wachter
authors.forename: Christiane
authors.initials: C
authors.lastname: Liers
authors.forename: René
authors.initials: R
authors.lastname: Ullrich
authors.forename: Martin
authors.initials: M
authors.lastname: Hofrichter
authors.forename: Dietmar A
authors.initials: DA
authors.lastname: Plattner
authors.forename: Klaus
authors.initials: K
authors.lastname: Piontek
mesh_terms: D000880:Anthraquinones / Q000737:chemistry*; D003116:Color; D004396:Coloring Agents / Q000737:chemistry*; D017124:Conserved Sequence; D005609:Free Radicals; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000737:chemistry*; D011485:Protein Binding; D014443:Tyrosine / Q000737:chemistry*
chemical_list: D000880:Anthraquinones; D004396:Coloring Agents; D005609:Free Radicals; D014443:Tyrosine; D010544:Peroxidases
keywords: Catalysis; Dye-decolorizing peroxidases (DyPs); Enzyme assay; Heme; Mass spectrometry; PROLI/NO; Spin trapping; Tryptophan; Tyrosine