2012
DOI: 10.4172/2329-6674.1000e105
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DyP-type Peroxidases: A Promising and Versatile Class of Enzymes

Abstract: Figure 1: Structural comparison of HRP from Armoracia rusticana (A) and DyP from Bjerkandera adusta Dec1 (C). α-helices are shown in red, β sheets are in yellow and the heme cofactor is in blue. Close-up of key amino acids in the heme-surrounding region of HRP (B) and DyP (D). The distal and proximal histidines (His42 and His170) as well as catalytically important residues (e.g. Arg38 and Phe41) of HRP are indicated. The proximal histidine (His308) and catalytically important residues (e.g. Arg39 and Asp171) o… Show more

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Cited by 6 publications
(3 citation statements)
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“…Furthermore, MnP is capable of oxidizing Mn 2+ to Mn 3+ , which is a diffusible oxidant capable of penetrating the cell wall matrix and degrading phenolic substrates (Hofrichter 2002 ). Otherwise, the Mn(II)-independent activity of some peroxidases also allows the oxidation of different compounds with a similar structure to synthetic dyes (Fraaije 2012 ), but with the advantage of not requiring the presence of manganese, which simplifies the biodegradation process. However, the major drawbacks of these enzymes for a wide industrial application are their high production cost and their limited yield (Elisashvili and Kachlishvili 2009 ).…”
Section: Introductionmentioning
confidence: 99%
“…Furthermore, MnP is capable of oxidizing Mn 2+ to Mn 3+ , which is a diffusible oxidant capable of penetrating the cell wall matrix and degrading phenolic substrates (Hofrichter 2002 ). Otherwise, the Mn(II)-independent activity of some peroxidases also allows the oxidation of different compounds with a similar structure to synthetic dyes (Fraaije 2012 ), but with the advantage of not requiring the presence of manganese, which simplifies the biodegradation process. However, the major drawbacks of these enzymes for a wide industrial application are their high production cost and their limited yield (Elisashvili and Kachlishvili 2009 ).…”
Section: Introductionmentioning
confidence: 99%
“…Peroxidases are oxidoreductases involved in a variety of biochemical processes, including the biosynthesis of cell wall material and immunological host-defense responses [1]. The recently discovered DyP-type peroxidases (DyPs, dye-decolorizing peroxidases; EC 1.11.1.19) represent a novel superfamily of heme-containing enzymes.…”
Section: Introductionmentioning
confidence: 99%
“…The lignin degradation process is further supported by other extracellular accessory enzymes, which include glucose oxidase (GLOX; EC 1.1.3.4), glyoxylate oxidase (EC 1.2.3.5), aryl-alcohol oxidase (AAO; EC 1.1.3.7), aryl-alcohol dehydrogenase (AAD; EC 1.1.1.90), and quinone reductases (EC 1.6.5.5) (Wong 2009;Dashtban et al 2010;Fraaije and van Bloois 2012;Pollegioni et al 2015;Stajić et al 2016;Falade et al 2017;Ceballos 2018).…”
Section: Lignin and Lignin-modifying Enzymesmentioning
confidence: 99%