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DyP-type peroxidases: a promising and versatile class of enzymes

Colpa, Dana I, Fraaije, Marco W, van Bloois, Edwin·2014·Journal of Industrial Microbiology and Biotechnology
DOI 10.1007/s10295-013-1371-6
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Abstract

DyP peroxidases comprise a novel superfamily of heme-containing peroxidases, which is unrelated to the superfamilies of plant and animal peroxidases. These enzymes have so far been identified in the genomes of fungi, bacteria, as well as archaea, although their physiological function is still unclear. DyPs are bifunctional enzymes displaying not only oxidative activity but also hydrolytic activity. Moreover, these enzymes are able to oxidize a variety of organic compounds of which some are poorly converted by established peroxidases, including dyes, β-carotene, and aromatic sulfides. Interestingly, accumulating evidence shows that microbial DyP peroxidases play a key role in the degradation of lignin. Owing to their unique properties, these enzymes are potentially interesting for a variety of biocatalytic applications. In this review, we deal with the biochemical and structural features of DyP-type peroxidases as well as their promising biotechnological potential.

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Fig. 1 Structural comparison of DyP from Bjerkandera adusta Dec1 ( a ), HRP from Armoracia rusticana ( b ), and human myeloperoxidase (hMPO) from Homo sapiens ( c ). α -helices are shown in green , β sheets are in blue , and the heme cofactor is in red . Close-up of key amino acids in the heme-surrounding region of DyP ( d ), HRP ( e ), and human myeloperoxidase ( f ). The proximal histidine of DyP (His308) and both the distal and proximal histidines of HRP (His42 and
Fig. 1 Structural comparison of DyP from Bjerkandera adusta Dec1 ( a ), HRP from Armoracia rusticana ( b ), and human myeloperoxidase (hMPO) from Homo sapiens ( c ). α -helices are shown in green , β sheets are in blue , and the heme cofactor is in red . Close-up of key amino acids in the heme-surrounding region of DyP ( d ), HRP ( e ), and human myeloperoxidase ( f ). The proximal histidine of DyP (His308) and both the distal and proximal histidines of HRP (His42 andCC-BY · From the PDF
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Research works printed but not linked: 50

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Metadata

Authors
Colpa, D. I., Fraaije, M. W., & van Bloois, E.
Venue
Journal of Industrial Microbiology and Biotechnology
Publisher
Oxford University Press (OUP)
Published
2014-01-01
Volume
41
Issue
1
Pages
1-7
ISSN
  • 1476-5535
  • 1367-5435
DOI
10.1007/s10295-013-1371-6
Cited by
203
References
0
Language
en
Licence
academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model (vor)

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