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Site-directed mutagenesis of manganese peroxidase from Phanerochaete chrysosporium in an in vitro expression system

Paper ID Volume ID Publish Year Pages File Format Full-Text
24889 43543 2009 3 PDF Available
Title
Site-directed mutagenesis of manganese peroxidase from Phanerochaete chrysosporium in an in vitro expression system
Abstract

An enzymatically active fungal manganese peroxidase (MnP) from Phanerochaete chrysosporium was synthesized in an in vitro coupled transcription–translation system. The synthesized MnP had the expected molecular mass (43,000 Da) and catalyzed the oxidation of 2,6-dimethoxyphenol (DMP) in the presence of hydrogen peroxide and Mn(II). A distal arginine residue (Arg 42) of the peroxide binding pocket and the potential N-glycosylation site (Asn 131) was site-directed mutagenized and corresponding mutant enzymes were also in vitro synthesized. Activities of the mutant enzymes towards 2,6-DMP were not significantly compromised although their dynamic characteristics were obviously different from the wild-type enzyme. The effect of the mutations was explained by using a computer-based three-dimensional modeling. These results demonstrated that in vitro expression of MnP provided a convenient and efficient system for characterization of fungal peroxidases.

Keywords
Manganese peroxidase; In vitro transcription and translation; Phanerochaete chrysosporium; Site-directed mutagenesis
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Site-directed mutagenesis of manganese peroxidase from Phanerochaete chrysosporium in an in vitro expression system
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 139, Issue 2, 15 January 2009, Pages 176–178
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
Online Support
Any Questions? feel free to contact us