Results 251 to 260 of about 61,259 (301)

Crystal structure of the ascorbate peroxidase–ascorbate complex

Nature Structural & Molecular Biology, 2003
Heme peroxidases catalyze the H2O2-dependent oxidation of a variety of substrates, most of which are organic. Mechanistically, these enzymes are well characterized: they share a common catalytic cycle that involves formation of a two-electron, oxidized Compound I intermediate followed by two single-electron reduction steps by substrate.
Sharp, K.H., Mewies, M., Moody, Peter C.E., Raven, E.L.   +3 more
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Common phylogeny of catalase-peroxidases and ascorbate peroxidases

Gene, 2000
Catalase-peroxidases belong to Class I of the plant, fungal, bacterial peroxidase superfamily, together with yeast cytochrome c peroxidase and ascorbate peroxidases. Obviously these bifunctional enzymes arose via gene duplication of an ancestral hydroperoxidase. A 230-residues long homologous region exists in all eukaryotic members of Class I, which is
M, Zámocký, S, Janecek, F, Koller
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The Redox Properties of Ascorbate Peroxidase

Biochemistry, 2007
Reduction potentials for the catalytic compound I/compound II and compound II/Fe3+ redox couples, and for the two-electron compound I/Fe3+ redox couple, have been determined for ascorbate peroxidase (APX) and for a number of site-directed variants.
Efimov, I, Papadopoulou, ND, McLean, KJ, Badyal, SK, Macdonald, IK, Munro, AW, Moody, PC, Raven, EL   +7 more
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Class I Heme Peroxidases: Characterization of Soybean Ascorbate Peroxidase

Archives of Biochemistry and Biophysics, 1998
An efficient expression system [D. A. Dalton et al. Arch. Biochem. Biophys. 328, 1-8, 1996) for soybean nodule ascorbate peroxidase (APX) has, for the first time, been used to generate enzyme in large enough quantities for detailed biophysical analysis. The recombinant APX has been characterized by electronic absorption, EPR, NMR and circular dichroism
Jones, DK, Raven, EL, Dalton, DA, Rosell, FI   +3 more
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Catalase-Peroxidases in Cyanobacteria – Similarities and Differences to Ascorbate Peroxidases

Free Radical Research, 1999
Cyanobacteria (blue-green algae) are oxygenic phototrophic bacteria carrying out plant-type photosynthesis. The only hydrogen peroxide scavenging enzymes in at least two unicellular species have been demonstrated to be bifunctional cytosolic catalase-peroxidases (CatPXs) having considerable homology at the active site with plant ascorbate peroxidases ...
C, Obinger, G, Regelsberger, P G, Furtmüller, C, Jakopitsch, F, Rüker, A, Pircher, G A, Peschek   +6 more
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Cytosolic ascorbate peroxidase in Gymnosperms

Plant Biosystems - An International Journal Dealing with all Aspects of Plant Biology, 2000
ABSTRACT Sixteen species of Gymnosperms have been screened for cytosolic ascorbate peroxidase by means of native polyacrylamide gel electrophoresis. This analysis shows that a single form of the enzyme is the most common situation. The enzyme reveals a similar electrophoretic mobility in species belonging to the same genus and sometimes to different ...
TOMMASI, Franca, PACIOLLA, Costantino
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Ascorbate Peroxidase in Malted Barley

Journal of the American Society of Brewing Chemists, 2013
An ascorbate peroxidase has been identified in the acrospire and aleurone of germinating barley. Its synthesis is triggered in the aleurone by the presence of ascorbic acid and hydrogen peroxide.
Makoto Kanauchi, Charles W. Bamforth
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Ascorbate peroxidase activity of cytochromec

Free Radical Research, 2010
The peroxidase-type reactivity of cytochrome c is proposed to play a role in free radical production and/or apoptosis. This study describes cytochrome c catalysis of peroxide consumption by ascorbate. Under conditions where the sixth coordination position at the cytochrome c heme iron becomes more accessible for exogenous ligands (by carboxymethylation,
Bischin, Cristina, Deac, Florina, Silaghi-Dumitrescu, Radu, Worrall, Jonathan AR, Rajagopal, Badri S, Damian, Grigore, Cooper, Chris E   +6 more
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Cross reactivity between ascorbate peroxidase and phenol (guaiacol) peroxidase

Postharvest Biology and Technology, 2014
Abstract Adverse conditions often induce an increase in active oxygen species (AOS) such as hydrogen peroxide (H 2 O 2 ). H 2 O 2 is converted to water, and thus becomes detoxified by enzymes such as ascorbate peroxidase (APX; EC 1.11.1.11). APX activity is estimated by the disappearance rate of ascorbic acid, which becomes oxidized.
Wouter G. van Doorn, Saichol Ketsa
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Soluble ascorbate peroxidase from potato tubers

Plant Science, 1992
Abstract Ascorbate peroxidase (EC 1.11.1.11) from potato tubers was purified to a nearly homogeneous state. The enzyme occurred only in the soluble fraction and showed to be labile in the absence of ascorbate. It had a r of ∼30 kDa, a pH optimum of ∼7, a K m for hydrogen peroxide of 30 μM and a K m for ascorbate of 55 μM.
Maria Rosaria Elia, Giuseppe Borraccino, Silvio Dipierro   +2 more
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