Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 537, Issue 2, Pages 161-167Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2013.07.007
Keywords
Catalysis; Dye-decolorizing peroxidases (DyPs); Enzyme assay; Heme; Mass spectrometry; PROLI/NO; Spin trapping; Tryptophan; Tyrosine
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Funding
- International Research Training Group IRTG 1038 Catalysts and Catalytic Reactions for Organic Synthesis (CCROS) of the Deutsche Forschungsgemeinschaft (DFG)
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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. (C) 2013 Elsevier Inc. All rights reserved.
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