Versatile peroxidase of Bjerkandera fumosa: Substrate and inhibitor specificity

Pozdnyakova, N. N.; Makarov, O. E.; Чернышова, М. П.; Turkovskaya, O. V.; Jarosz-Wilkołazka, Anna

doi:10.1016/j.enzmictec.2012.10.005

Cited by 23 publications

(14 citation statements)

References 58 publications

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“…VPPO oxidised the typical VP substrates including VA and Mn 2 ϩ (Table I). However, we did not fi nd the biphasic kinetics with apparent saturation in both micromolar and millimolar ranges during VPPO oxidation of 2,7-diaminofl uorene as seen in VPBF oxidation of this substrate (Pozdnyakova et al 2013). In the case of ABTS, no inhibition of VPPO activity by an excess of the substrate was observed, as seen in previous studies on VPBF (Pozdnyakova et al 2013).…”

Section: Resultssupporting

confidence: 51%

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Decolourisation of anthraquinone-and anthracene-type dyes by versatile peroxidases frombjerkandera fumosa and pleurotus ostreatusD1

Pozdnyakova

Jarosz-Wilkołazka

Polak

et al. 2015

Biocatalysis and Biotransformation

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The catalytic properties of a versatile peroxidase from Pleurotus ostreatus D1 (Jacquin) P. Kummer were studied in comparison with that of a typical versatile peroxidase from Bjerkandera fumosa 137 (Per.:Fr) Karst. Decolourisation activities of both enzymes towards a wide range of dyes containing condensed aromatic rings (anthraquinone-and anthracene-type) were found. The anthraquinone dyes were decolourised rapidly by both tested peroxidases. The presence of polymerisation reaction products of Acid Blue 62, Basic Blue 22 and Reactive Blue 4 oxidation, and breakdown of aromatic rings of Alizarin Red were observed. The main catalytic constants ( K M and V max ) of the decolourisation reactions of anthraquinone dyes were calculated. In the case of Alizarin Red, inhibition of the activity of versatile peroxidase from P. ostreatus D1 by an excess of the substrate was observed. Independence from Mn 2 ϩ ions of the catalytic activity of versatile peroxidase from P. ostreatus D1 towards different substrates was revealed. Finally, differences in the catalytic activity towards anthracenetype dyes and monoaromatic substrates of both peroxidases were found.

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Section: Resultssupporting

confidence: 51%

“…Karst. (VPBF) was purifi ed and characterised in previous work (Pozdnyakova et al 2013). Based on the main catalytic properties (oxidation of VA and DMP, both with and without MnCl 2 , and direct oxidation of Mn 2 ϩ ions) (Table I), this enzyme was identifi ed as a typical VP (Pozdnyakova et al 2013).…”

Section: Resultsmentioning

confidence: 99%

Decolourisation of anthraquinone-and anthracene-type dyes by versatile peroxidases frombjerkandera fumosa and pleurotus ostreatusD1

Pozdnyakova

Jarosz-Wilkołazka

Polak

et al. 2015

Biocatalysis and Biotransformation

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“…The biotechnological use of the catalytic potential of peroxidases should be built on broad-scale studies addressing substrate specificity and the effectors influencing their activities. Enzymatic biocatalysis plays a very important role in the development of many chemical industries, e.g., energy, food or fine chemistry [15].…”

Section: Introductionmentioning

confidence: 99%

Kinetics of Spanish broom peroxidase obeys a Ping-Pong Bi–Bi mechanism with competitive inhibition by substrates

Galende

Cuadrado

Kostetsky

et al. 2015

International Journal of Biological Macromolecules

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“…Indeed, as stated earlier, we made a similar oxidation product of an analog compound using a commercial peroxidase. However, the oxidation of AZD9819 in plasma is not inhibited by sodium azide (NaN 3 ; Table 2), a known inhibitor of peroxidases (Ortiz de Montellano, 1992;Pozdnyakova et al, 2013). We also excluded xanthine oxidase (XO).…”

Section: Vs C) This Indicates That the Incorporatedmentioning

confidence: 99%

Lipid Peroxide–Mediated Oxidative Rearrangement of the Pyrazinone Carboxamide Core of Neutrophil Elastase Inhibitor AZD9819 in Blood Plasma Samples

Lewis

Wells

et al. 2015

Drug Metab Dispos

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This study focused on the mechanistic interpretation of ex vivo oxidation of a candidate drug in blood plasma samples. An unexpected lipid peroxide-mediated epoxidation followed by a dramatic rearrangement led to production of a five-membered oxazole derivative from the original six-membered pyrazinone-carboxamide core of a human neutrophil elastase inhibitor, 6-(1-(4-cyanophenyl)-oxazole-4-carboxamide was characterized by accurate-mass tandem mass spectrometry fragmentations, by two-dimensional NMR and X-ray crystallography of an authentic standard, and by incorporation of an 18 O atom from molecular 18 O 2 to the location predicted by our proposed mechanism. The lipid peroxide-mediated oxidation was demonstrated by using human low-density lipoprotein (LDL) in pH 7.4 phosphate buffer and by inhibiting the oxidation with ascorbic acid or L-glutathione, two antioxidants effective in both plasma and the LDL incubation. A nucleophilic mechanism for the epoxidation of AZD9819 by lipid hydroperoxides explains the prevention of its ex vivo oxidation by acidification of the plasma samples. The discovery of the lipid peroxide-dependent oxidation of an analyte and the means of prevention could provide valuable information for biotransformation and bioanalysis.

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Versatile peroxidase of Bjerkandera fumosa: Substrate and inhibitor specificity

Cited by 23 publications

References 58 publications

Decolourisation of anthraquinone-and anthracene-type dyes by versatile peroxidases frombjerkandera fumosa and pleurotus ostreatusD1

Decolourisation of anthraquinone-and anthracene-type dyes by versatile peroxidases frombjerkandera fumosa and pleurotus ostreatusD1

Kinetics of Spanish broom peroxidase obeys a Ping-Pong Bi–Bi mechanism with competitive inhibition by substrates

Lipid Peroxide–Mediated Oxidative Rearrangement of the Pyrazinone Carboxamide Core of Neutrophil Elastase Inhibitor AZD9819 in Blood Plasma Samples

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