Difference between revisions of "Part:BBa K500000"
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<partinfo>BBa_K500000 parameters</partinfo> | <partinfo>BBa_K500000 parameters</partinfo> | ||
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+ | = ''Updated by NPU - CHINA 2022 '' == | ||
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+ | Lignin peroxidases have the unique ability to catalyze oxidative cleavage of C–C bonds and ether (C–O–C) bonds in non-phenolic aromatic substrates of high redox potential. | ||
+ | In our project(BBa_K4309001), Lignin peroxidase LipH8 from Phanerochaete chrysosporium was overexpressed in E. coli for the remediation of PAHs. |
Revision as of 16:37, 11 October 2022
lignin degradation 1
Yeast codon optimization , no terminator codon, from Phanerochaete chrysosporium. Synthetized by Geneart Lignin peroxidase (Lip) is a monomeric haemoglycoprotein secreted by wood-degrading fungi, such as the white wood-rot fungus Phanerochaete chrysosporium. Lignin peroxidases are of interest in waste treatment process and in catalysing difficult chemical transformations.
Sequence and Features
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Updated by NPU - CHINA 2022 =
Lignin peroxidases have the unique ability to catalyze oxidative cleavage of C–C bonds and ether (C–O–C) bonds in non-phenolic aromatic substrates of high redox potential. In our project(BBa_K4309001), Lignin peroxidase LipH8 from Phanerochaete chrysosporium was overexpressed in E. coli for the remediation of PAHs.