Difference between revisions of "Part:BBa K2685001"
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| − | Manganese peroxidase (MnP) is the most common lignin-modifying peroxidase produced by almost all wood-colonizing basidiomycetes causing white-rot and various soil-colonizing litter-decomposing fungi. Multiple forms of this glycosylated heme protein with molecular weights normally at 40 to 50 kDa are secreted by ligninolytic fungi into their microenvironment. There, MnP preferentially oxidizes manganese(II) ions (Mn2+), always present in wood and soils, into highly reactive Mn3+, which is stabilized by fungal chelators such as oxalic acid. Chelated Mn3+ in turn acts as low-molecular weight, diffusible redox-mediator that attacks phenolic lignin structures resulting in the formation of instable free radicals that tend to disintegrate spontaneously. MnP is capable of oxidizing and depolymerizing natural and synthetic lignins as well as entire lignocelluloses (milled straw or wood, pulp) in cell-free systems (in vitro). In vitro depolymerization is enhanced in the presence of co-oxidants such as thiols (e.g. glutathione) or unsaturated fatty acids and their derivatives | + | <p>Manganese peroxidase (MnP) is the most common lignin-modifying peroxidase produced by almost all wood-colonizing basidiomycetes causing white-rot and various soil-colonizing litter-decomposing fungi. Multiple forms of this glycosylated heme protein with molecular weights normally at 40 to 50 kDa are secreted by ligninolytic fungi into their microenvironment. There, MnP preferentially oxidizes manganese(II) ions (Mn2+), always present in wood and soils, into highly reactive Mn3+, which is stabilized by fungal chelators such as oxalic acid. Chelated Mn3+ in turn acts as low-molecular weight, diffusible redox-mediator that attacks phenolic lignin structures resulting in the formation of instable free radicals that tend to disintegrate spontaneously. MnP is capable of oxidizing and depolymerizing natural and synthetic lignins as well as entire lignocelluloses (milled straw or wood, pulp) in cell-free systems (in vitro). In vitro depolymerization is enhanced in the presence of co-oxidants such as thiols (e.g. glutathione) or unsaturated fatty acids and their derivatives .</p> |
| − | + | <p> In this year, we use this special peroxidase to degradate the tetracycline in the degradation parts.We also have optimized this enzyme condon to better express in our constructive chasis.</p> | |
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Latest revision as of 20:52, 17 October 2018
Manganese Peroxidases
Manganese peroxidase (MnP) is the most common lignin-modifying peroxidase produced by almost all wood-colonizing basidiomycetes causing white-rot and various soil-colonizing litter-decomposing fungi. Multiple forms of this glycosylated heme protein with molecular weights normally at 40 to 50 kDa are secreted by ligninolytic fungi into their microenvironment. There, MnP preferentially oxidizes manganese(II) ions (Mn2+), always present in wood and soils, into highly reactive Mn3+, which is stabilized by fungal chelators such as oxalic acid. Chelated Mn3+ in turn acts as low-molecular weight, diffusible redox-mediator that attacks phenolic lignin structures resulting in the formation of instable free radicals that tend to disintegrate spontaneously. MnP is capable of oxidizing and depolymerizing natural and synthetic lignins as well as entire lignocelluloses (milled straw or wood, pulp) in cell-free systems (in vitro). In vitro depolymerization is enhanced in the presence of co-oxidants such as thiols (e.g. glutathione) or unsaturated fatty acids and their derivatives .
In this year, we use this special peroxidase to degradate the tetracycline in the degradation parts.We also have optimized this enzyme condon to better express in our constructive chasis.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 1126
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 957
Illegal AgeI site found at 706
Illegal AgeI site found at 751
Illegal AgeI site found at 949
Illegal AgeI site found at 979 - 1000COMPATIBLE WITH RFC[1000]