Manganese peroxidase MnP

Figure 7. N-terminal sequence for the first 47 amino acids of the manganese peroxidase (MnP) isolated from L. edodes cultures own on a commercial wood medium and homology with the deduced amino acid sequences for the MnP s or lignin peroxidases (LP s) reported from P. chrysosporium. Boxed areas show regions of sequence identity. Homology is the total length of identical or conservative substitutions. (Reproduced with permission from ref. 15. Copyright 1990 Springer-Verlag.)...

Figure 2. Comparison of P. chrysosporium MnP-1 and other peroxidases at regions near the proximal and distal histidines. The peroxidase sequences used were manganese peroxidase (MnP) (20), cytochrome c peroxidase (CCP) QS), horseradish peroxidase (HRP)...

Michel, F.C.J. Dass, S.B. Grulke, E.A. Reddy, C.A. Role of manganese peroxidases (MNP) and lignin peroxidases (LiP) of Phanerochaete chrysosporium in the decolorization of Kraft bleach plant effluent. Appl. Environ. Microbiol. 1991, 57, 2368-2375. 

White-rot fungi produce three peroxidases that are involved in lignin degradation, namely, lignin peroxidase (LiP) and manganese peroxidase (MnP), first discovered in Phanerochaete chrysosporium in the 1980s, and versatile peroxidase (VP),... 

Fig. 2.11 Phylogeny of Class II of the peroxidase-catalase superfamily. Sequences coding for secretory fungal peroxidases lignin peroxidase (LiP), manganese peroxidase (MnP), and versatile peroxidase (VP) were used for this reconstruction. One of nine equally parsimonious trees is presented. Bootstrap values are indicated before slash, and Bayesian posterior probability values are indicated after the slash. With kind permission from Springer Science Business Media Morgenstem et al. [32], Fig. 2...

Hofrichter M (2002) Review Lignin conversion by manganese peroxidase (MnP). Enzyme Microb Technol 30 454-466... 

Mielgo I, Palma C, Guisan JM et al (2003) Covalent immobilisation of manganese peroxidases (MnP) from Phanerochaete chrysosporium and Bjerkandera sp. BOS55. Enzyme Microb Technol 32 769-775... 

Batch reactors based on peroxidases are mainly applied for degradation purposes (see Chap. 8). LiP, manganese peroxidase (MnP), HRP, SBP, and CPO were used for the oxidation of phenolic compounds [3, 6, 7, 9, 20, 38, 74, 75, 95], decoloriza-tion of dye-containing effluents [5, 22], and pulp biobleaching [59]. In the field of synthesis, CPO is the most versatile and promising of the peroxidases (see Chap. 6). It was applied in discontinuous operation for epoxidations [78,79], enantioselective oxidations of alcohols to aldehydes [14,48], halogenations [77,80], hydroxylations, and oxidation of indole to oxindole, which is an important drug precursor [96]. 

The white rot basidiomycete Phanerochaete chrysosporium secretes two soluble H202-requiring peroxidases which are Involved in lignin degradation. Both lignin peroxidase (LIP) and manganese peroxidase (MnP) form the oxidized intermediates compound 1 and compound II. 

Mn Peroxidase. The manganese peroxidase (MnP) is one of the two known enzymes capable of the oxidative degradation of lignin, an amorphous, random, aromatic polymer synthesized from p-hydroxycin-namyl alcohol, 4-hydroxy-3-methoxycinnamyl alcohol, and 3,5,-dime-thoxy-4-hydroxycinnamyl alcohol precursors by woody plants. Both enzymes contain the protoporphyrin IX heme prosthetic group, similar to the heme peroxidases with an L5-histidine and both use hydrogen peroxide as a substrate. However, the manganese peroxidase has an absolute requirement for Mn(II) to complete its catalytic cycle (50). The X-ray structure of this protein has recently appeared (51). 

Figure 5 Schematic diagram showing the heme environment and Mn-binding site of manganese peroxidase (MnP)...

Creation of a New Mn(II)-binding Site in Peroxidases Toward A New Manganese Peroxidase. Cytochrome c peroxidase (CcP) and manganese peroxidase (MnP) are... 

Several lines of evidence indicate that manganese peroxidase (MnP) is a key enzyme in pulp bleaching by T. versicolor. The enzyme is indnced by the presence of pulp (Figure 15.7) [108], as are organic acids that are reqnired for chelation of Mn(III)... 

Manganese peroxidase (MnP) is an unique enzyme in many respects. It is an extracellular enzyme that involves a heme protoporphyrin IX for the oxidation of Mn" to Mn " 94, 95). A crystal structure at 2.06-A resolution of the manganese peroxidase from the white rot basidiomycete Phanerocaete chrysosporium, which utilizes this enzyme to degrade lignin, appeared in 1994 96). The active site (Fig. 5) and the overall structure are quite similar to lignin peroxidase (LiP),... 

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