Manganese Peroxidase from Phanerochaete chrysosporium. A Homology-Based Molecular Model
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چکیده
منابع مشابه
Manganese-dependent Peroxidase from Phanerochaete chrysosporium
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...
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Production of manganese-dependent peroxidase (MnP) by the white-rot fungus Phanerochaete chrysosporium BKMF-1767 (ATCC 24725) was monitored during growth in different media and growth conditions. The effect of some activators of MnP production, Mn, Tween 80, phenylmethylsulphonylfloride (PMSF), oxygen, temperature, pH, glycerol and nitrogen was studied. Supplementing the cultures with Tween 80 ...
متن کاملHomologous expression of recombinant manganese peroxidase in Phanerochaete chrysosporium.
The promoter region of the glyceraldehyde-3-phosphate dehydrogenase gene (gpd) was used to drive expression of mnp1, the gene encoding Mn peroxidase isozyme 1, in primary metabolic cultures of Phanerochaete chrysosporium. A 1,100-bp fragment of the P. chrysosporium gpd promoter region was fused upstream of the mnp1 gene to construct plasmid pAGM1, which contained the Schizophyllum commune ade5 ...
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...
متن کاملThe crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06-A resolution.
The crystal structure of manganese peroxidase (MnP) from the lignin-degrading basidiomycetous fungus Phanerochaete chrysosporium has been solved using molecular replacement techniques and refined to R = 0.20 at 2.0 A. The overall structure is similar to that of two other fungal peroxidases, lignin peroxidase from P. chrysosporium and Arthromyces ramosus peroxidase. Like the other fungal peroxid...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1995
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1995.0955m.x