Download Biocatalysis Based on Heme Peroxidases: Peroxidases as by Eduardo Torres, Marcela Ayala PDF

By Eduardo Torres, Marcela Ayala

This monograph describes many functions of peroxidase-based biocatalysis within the biotechnology undefined. the necessity for this type of publication emerges from the massive volume of recent facts concerning the phylogeny, response mechanisms, thermodynamic characterization and structural good points of fungal and plant heme peroxidases that has been generated some time past 10 years, because the final really expert ebook on peroxidases was once released. the purpose of this publication is to offer contemporary advances on such easy elements as evolution, structure-function relation and catalytic mechanism in addition to utilized points, corresponding to bioreactor and protein engineering, to supply the instruments for rational layout of more suitable biocatalysts and biocatalytic approaches.

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Extra info for Biocatalysis Based on Heme Peroxidases: Peroxidases as Potential Industrial Biocatalysts

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55 Abstract This chapter begins with a description of the main structural features of heme peroxidases representative of the two large superfamilies of plant–fungal– bacterial and animal peroxidases, and the four additional (super)families described to date. Then, we focus on several fungal peroxidases of high biotechnological potential as industrial biocatalysts. These include (1) ligninolytic peroxidases from white-rot basidiomycetes being able to oxidize high redox-potential substrates at an exposed protein radical; (2) heme-thiolate peroxidases that are structural hybrids of typical peroxidases and cytochrome P450 enzymes and, after their discovery in sooty molds, are being described in basidiomycetes with even more interesting catalytic properties, such as selective aromatic oxygenation; and (3) the socalled dye-decolorizing peroxidases that are still to be thoroughly investigated but have been identified in different basidiomycete genomes.

T. Martı´nez 46 Interestingly, CIP clusters with three other low redox-potential peroxidases from Coprinellus disseminatus, and from the genomes of P. chrysosporium (NOP) [44] and Postia placenta [36] (group D), being distantly related to the above large group of ligninolytic peroxidases. The remaining 21 peroxidases form three groups (evolutionarily very distant from the rest) that include some interesting enzymes, together with basidiomycete CCP (group E). The group of CPO-type peroxidases (F) is formed by two Agrocybe aegerita heme-thiolate peroxidases clustered with a similar peroxidase from A.

The total number of Class III genes entered in PeroxiBase exceeds already 3,000 (January 2010) thus representing over 73% of all entered superfamily members. Monocotyledon peroxidases differ slightly in their sequence fingerprints from Eudicotyledons counterparts [50], but the majority of the prx genes is highly conserved throughout the whole Class III. The observed overall sequence similarities lead to the classification of all available 2 Molecular Phylogeny of Heme Peroxidases 25 Class III peroxidases in eight distinct groups [50], the most abundant in rice being group I and IV.

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