Substrate oxidation sites in versatile peroxidase and other basidiomycete peroxidases
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چکیده
منابع مشابه
Substrate oxidation sites in versatile peroxidase and other basidiomycete peroxidases.
Versatile peroxidase (VP) is defined by its capabilities to oxidize the typical substrates of other basidiomycete peroxidases: (i) Mn(2+), the manganese peroxidase (MnP) substrate (Mn(3+) being able to oxidize phenols and initiate lipid peroxidation reactions); (ii) veratryl alcohol (VA), the typical lignin peroxidase (LiP) substrate; and (iii) simple phenols, which are the substrates of Coprin...
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Trypanosoma brucei, the causative agent of African sleeping sickness, encodes three nearly identical cysteine homologues of the classical selenocysteine-containing glutathione peroxidases. Although one of the sequences, peroxidase III, carries both putative mitochondrial and glycosomal targeting signals, the proteins are detectable only in the cytosol and mitochondrion of mammalian bloodstream ...
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Versatile peroxidase shares with manganese peroxidase and lignin peroxidase the ability to oxidize Mn(2+) and high redox potential aromatic compounds, respectively. Moreover, it is also able to oxidize phenols (and low redox potential dyes) at two catalytic sites, as shown by biphasic kinetics. A high efficiency site (with 2,6-dimethoxyphenol and p-hydroquinone catalytic efficiencies of ∼70 and...
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The physical properties and activities of the purified catalase-peroxidase hydroperoxidase I (HPI) of Escherichia coli (EcHPI) and HPI with a carboxyl-terminal extension of Mycobacterium tuberculosis (MtHPI-e) are compared to those of commercial preparations of horseradish peroxidase (HRP). The catalase-peroxidase proteins had similar absorption spectra and differed primarily in that MtHPI-e ha...
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Manganese oxidation by manganese peroxidase (MnP) was investigated. Stoichiometric, kinetic, and Mn" binding studies demonstrated that MnP has a single manganese binding site near the heme, and two Mn"' equivalents are formed at the expense of one H202 equivalent. Since each catalytic cycle step is irreversible, the data fit a peroxidase ping-pong mechanism rather than an ordered bi-bi ping...
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ژورنال
عنوان ژورنال: Journal of Experimental Botany
سال: 2009
ISSN: 0022-0957,1460-2431
DOI: 10.1093/jxb/ern261