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染料脱色过氧化物酶的多彩调色板。

The multihued palette of dye-decolorizing peroxidases.

作者信息

Singh Rahul, Eltis Lindsay D

机构信息

Department of Microbiology & Immunology, The University of British Columbia, Life Sciences Institute, Vancouver, BC V6T 1Z3, Canada.

Department of Microbiology & Immunology, The University of British Columbia, Life Sciences Institute, Vancouver, BC V6T 1Z3, Canada; Department of Biochemistry & Molecular Biology, The University of British Columbia, Life Sciences Institute, Vancouver, BC V6T 1Z3, Canada.

出版信息

Arch Biochem Biophys. 2015 May 15;574:56-65. doi: 10.1016/j.abb.2015.01.014. Epub 2015 Mar 2.

DOI:10.1016/j.abb.2015.01.014
PMID:25743546
Abstract

Dye-decolorizing peroxidases (DyPs; EC 1.11.1.19) are heme enzymes that comprise a family of the dimeric α+β barrel structural superfamily of proteins. The first DyP, identified relatively recently in the fungus Bjerkandera adusta, was characterized for its ability to catalyze the decolorization of anthraquinone-based industrial dyes. These enzymes are now known to be present in all three domains of life, but do not appear to occur in plants or animals. They are involved in a range of physiological processes, although in many cases their roles remain unknown. This has not prevented the development of their biocatalytic potential, which includes the transformation of lignin. This review highlights the functional diversity of DyPs in the light of phylogenetic, structural and biochemical data. The phylogenetic analysis reveals the existence of at least five classes of DyPs. Their potential physiological roles are discussed based in part on synteny analyses. Finally, the considerable biotechnological potential of DyPs is summarized.

摘要

染料脱色过氧化物酶(DyPs;EC 1.11.1.19)是一类血红素酶,属于二聚体α+β桶状结构超家族蛋白质。首个DyP是最近在真菌烟管菌中发现的,其特征在于能够催化蒽醌类工业染料的脱色。现在已知这些酶存在于生命的所有三个域中,但似乎不存在于植物或动物中。它们参与一系列生理过程,尽管在许多情况下它们的作用仍然未知。这并没有阻止其生物催化潜力的开发,其中包括木质素的转化。本综述根据系统发育、结构和生化数据突出了DyPs的功能多样性。系统发育分析揭示了至少五类DyPs的存在。部分基于共线性分析讨论了它们潜在的生理作用。最后,总结了DyPs巨大的生物技术潜力。

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