Kinetic analysis of manganese peroxidase. The reaction with manganese complexes.
نویسندگان
چکیده
منابع مشابه
Effect of manganese on the secretion of manganese-peroxidase by the basidiomycete Ceriporiopsis subvermispora.
The ligninolytic machinery of the widely used model fungus Ceriporiopsis subvermispora includes the enzymes manganese-peroxidase (MnP) and laccase (Lcs). In this work the effect of Mn(II) on the secretion of MnP was studied. Cultures grown in the absence of Mn(II) showed high levels of mnp transcripts. However, almost no MnP enzyme was detected in the extracellular medium, either by enzymatic a...
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A cDNA clone encoding a manganese-dependent peroxidase from the filamentous fungus Phanerochaete chrysosporium was isolated and characterized. The clone, AMP-1, was isolated by screening a X g t l l expression library with polyclonal antibodies raised against a purified manganese-dependent peroxidase (isozyme H4, PI 4.5). The XMP-1 cDNA sequence predicts a mature protein containing 358 amino a...
متن کاملManganese(I1) Oxidation by Manganese Peroxidase from the Basidiomycete Phanerochaete chrysosporium
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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BACKGROUND Manganese-binding sites are found in several heme peroxidases, namely manganese peroxidase (MnP), chloroperoxidase, and the cationic isozyme of peanut peroxidase. The Mn-binding site in MnP is of particular interest. Oxidation of Mn(II) to Mn(III) is a key step in the biodegradation of lignin, a complex phenylpropanoid polymer, as well as many aromatic pollutants. Cytochrome c peroxi...
متن کاملMagnetic resonance and kinetic studies related to the manganese activation of the adenylate kinase reaction.
Proton relaxation rate (PRR) studies indicated that there was little direct interaction between manganous ion and adenylate kinase. However, a large enhancement of the PRR of water was observed in the presence of ATP; for the enzyme combined with manganous-ATP complex rather than directly with the metal ion. Thus adenylate kinase is similar to creatine kinase but not to pyruvate kinase, with re...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1993
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(20)80694-2