Oxidation reactions catalyzed by manganese peroxidase isoenzymes from <i>Ceriporiopsis subvermispora</i>

Urzúa, Ulises; Larrondo, Luis F.; Lobos, Sergio; Larraı́n, Juan; Vicuña, Rafael

doi:10.1016/0014-5793(95)00874-9

Cited by 65 publications

(42 citation statements)

References 30 publications

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“…The physical characteristics in terms of molecular mass, isoelectric point, and heme absorbance of the purified MnP do not differ from those of other MnP isozymes described from other white rot fungi (32)(33)(34)(35). The turnover number of Mn(II) oxidation by MnP from Bjerkandera sp.…”

Section: Discussionmentioning

confidence: 65%

“…The addition of glycolate stimulated the production of several heme peaks. However, most of the MnP activity was attributed to one peak (fractions [33][34][35]. In other studies with glycolate and other organic acids (data not shown), the MnP activity was sometimes distributed between two major peaks: fractions 33-35 and 38 -39, respectively.…”

Section: Mnp Production In the Cultures Of Bjerkandera Sp Strainmentioning

confidence: 93%

“…Proteins were eluted with a linear gradient of sodium acetate up to 450 mM (pH 6.0) in 45 min, and 1-ml fractions were collected (1 ml/min) for 45 min. The fractions, [33][34][35], that contained the most MnP activity were collected and then washed and concentrated by ultrafiltration. The concentrate was eluted by creating a decreasing pH gradient in the pH range of 4.5-2.7 on a MonoP chromatofocusing column (Pharmacia) as described earlier (25), and 1-ml fractions were collected (1 ml/min) for 40 min.…”

Section: Methodsmentioning

confidence: 99%

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Characterization of a Novel Manganese Peroxidase-Lignin Peroxidase Hybrid Isozyme Produced by Bjerkandera Species Strain BOS55 in the Absence of Manganese

Mester

Field

1998

Journal of Biological Chemistry

254

121

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Section: Discussionmentioning

confidence: 65%

Section: Mnp Production In the Cultures Of Bjerkandera Sp Strainmentioning

confidence: 93%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Characterization of a Novel Manganese Peroxidase-Lignin Peroxidase Hybrid Isozyme Produced by Bjerkandera Species Strain BOS55 in the Absence of Manganese

Mester

Field

1998

Journal of Biological Chemistry

254

121

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“…The final purification step in an anion exchanger (MonoQ column) resulted in two fractions with the same molecular mass, thus indicating the presence of two isoforms. Isoforms with almost identical molecular masses were reported for other UPOs (e.g., UPOs of A. aegerita and C. radians ) and fungal heme peroxidases (e.g., manganese peroxidases of Ceriporiopsis subvermispora ) 14, 15, 16, 37…”

Section: Discussionmentioning

confidence: 68%

A Peroxygenase from Chaetomium globosum Catalyzes the Selective Oxygenation of Testosterone

et al. 2017

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Unspecific peroxygenases (UPO, EC 1.11.2.1) secreted by fungi open an efficient way to selectively oxyfunctionalize diverse organic substrates, including less‐activated hydrocarbons, by transferring peroxide‐borne oxygen. We investigated a cell‐free approach to incorporate epoxy and hydroxyl functionalities directly into the bulky molecule testosterone by a novel unspecific peroxygenase (UPO) that is produced by the ascomycetous fungus Chaetomium globosum in a complex medium rich in carbon and nitrogen. Purification by fast protein liquid chromatography revealed two enzyme fractions with the same molecular mass (36 kDa) and with specific activity of 4.4 to 12 U mg−1. Although the well‐known UPOs of Agrocybe aegerita (AaeUPO) and Marasmius rotula (MroUPO) failed to convert testosterone in a comparative study, the UPO of C. globosum (CglUPO) accepted testosterone as substrate and converted it with total turnover number (TTN) of up to 7000 into two oxygenated products: the 4,5‐epoxide of testosterone in β‐configuration and 16α‐hydroxytestosterone. The reaction performed on a 100 mg scale resulted in the formation of about 90 % of the epoxide and 10 % of the hydroxylation product, both of which could be isolated with purities above 96 %. Thus, CglUPO is a promising biocatalyst for the oxyfunctionalization of bulky steroids and it will be a useful tool for the synthesis of pharmaceutically relevant steroidal molecules.

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“…Substantial evidence implicates MnP involvement (7,8) GH1 GH2 GH3 GH5 GH6 GH7 GH9 GH10 GH11 GH12 GH13 GH15 GH16 GH17 GH18 GH20 GH23 GH25 GH115 GH95 GH92 GH89 GH88 GH85 GH79 GH61 GH63 GH71 GH72 GH74 GH78 GH55 GH53 GH47 GH45 GH43 GH38 GH37 GH35 GH31 GH30 GH28 GH27 GH105 Fig. 3.…”

Section: Other Enzymes Potentially Involved In Extracellular Redox Prmentioning

confidence: 99%

Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete chrysosporium provide insight into selective ligninolysis

Fernández‐Fueyo

Ruíz-Dueñas

Ferreira

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

270

235

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Efficient lignin depolymerization is unique to the wood decay basidiomycetes, collectively referred to as white rot fungi. Phanerochaete chrysosporium simultaneously degrades lignin and cellulose, whereas the closely related species, Ceriporiopsis subvermispora, also depolymerizes lignin but may do so with relatively little cellulose degradation. To investigate the basis for selective ligninolysis, we conducted comparative genome analysis of C. subvermispora and P. chrysosporium . Genes encoding manganese peroxidase numbered 13 and five in C. subvermispora and P. chrysosporium , respectively. In addition, the C. subvermispora genome contains at least seven genes predicted to encode laccases, whereas the P. chrysosporium genome contains none. We also observed expansion of the number of C. subvermispora desaturase-encoding genes putatively involved in lipid metabolism. Microarray-based transcriptome analysis showed substantial up-regulation of several desaturase and MnP genes in wood-containing medium. MS identified MnP proteins in C. subvermispora culture filtrates, but none in P. chrysosporium cultures. These results support the importance of MnP and a lignin degradation mechanism whereby cleavage of the dominant nonphenolic structures is mediated by lipid peroxidation products. Two C. subvermispora genes were predicted to encode peroxidases structurally similar to P. chrysosporium lignin peroxidase and, following heterologous expression in Escherichia coli , the enzymes were shown to oxidize high redox potential substrates, but not Mn 2+ . Apart from oxidative lignin degradation, we also examined cellulolytic and hemicellulolytic systems in both fungi. In summary, the C. subvermispora genetic inventory and expression patterns exhibit increased oxidoreductase potential and diminished cellulolytic capability relative to P. chrysosporium .

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Oxidation reactions catalyzed by manganese peroxidase isoenzymes from Ceriporiopsis subvermispora

Abstract: MnPs from this fungus are able to oxidize kojic acid without externally added hydrogen peroxide, indicating that they can also act as oxidases. In this reaction, however, the requirement for Mn(II) is absolute.

Cited by 65 publications

References 30 publications

Characterization of a Novel Manganese Peroxidase-Lignin Peroxidase Hybrid Isozyme Produced by Bjerkandera Species Strain BOS55 in the Absence of Manganese

Characterization of a Novel Manganese Peroxidase-Lignin Peroxidase Hybrid Isozyme Produced by Bjerkandera Species Strain BOS55 in the Absence of Manganese

A Peroxygenase from Chaetomium globosum Catalyzes the Selective Oxygenation of Testosterone

Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete chrysosporium provide insight into selective ligninolysis

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