Institute of Organic Chemistry, Albert-Ludwigs-University, Albertstrasse 21, 79104 Freiburg, Germany.
Arch Biochem Biophys. 2013 Sep 15;537(2):161-7. doi: 10.1016/j.abb.2013.07.007. Epub 2013 Jul 19.
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.
漆酶过氧化物酶 (DyP) 能够切断体积庞大的蒽醌染料。最近发表的 AauDyPI 晶体结构表明，大多数 DyP 底物不能直接在远端血红素腔中进行氧化。研究表明，一个暴露在表面的酪氨酸残基充当了体积庞大的底物的相互作用位点。这种氨基酸在真核 DyP 中是保守的，但在结构上相关的亚氯酸盐歧化酶 (Clds) 中却缺失。原核来源的漆酶过氧化物酶在多肽的相同区域同样具有保守的酪氨酸，尽管位置并不相同。
