Structure of Thermobifida fusca DyP-type peroxidase and activity towards Kraft lignin and lignin model compounds
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- 作者：Rahman Rahmanpoura ; Dean Reab ; Shirin Jamshidia ; Vilmos Fü ; lö ; pb ; Timothy D.H. Bugga ; T.D.Bugg@warwick.ac.uk" class="auth_mail" title="E-mail the corresponding author
- 关键词：Dye decolorizing peroxidase ; Dyp ; Lignin oxidation ; Protein crystallography
- 刊名：Archives of Biochemistry and Biophysics
- 出版年：2016
- 出版时间：15 March 2016
- 年：2016
- 卷：594
- 期：Complete
- 页码：54-60
- 全文大小：1056 K
文摘
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Thermobifida fusca DyP peroxidase is found to show activity for lignin oxidation.
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Oxidation of a β-aryl ether lignin model compound yields an oxidised dimer.
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The crystal structure of this enzyme was determined to 1.8 Å resolution.
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Site-directed mutagenesis of active site residues Asp-203 and Arg-315 was carried out, in order to study catalytic function.