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Literature summary for 1.11.1.14 extracted from
- Microbial lignin peroxidases applications, production challenges and future perspectives (2020), Enzyme Microb. Technol., 141, 109669 .
Application
| Application | Comment | Organism |
|---|---|---|
| biofuel production | the use of LiP may provide a cost-effective, efficient and greener route for the transformation of biomass into second-generation (2 G) biofuels. Lignin depolymerization is an important step in producing 2 G biofuels and other green chemicals as lignin protects cellulose and hemicellulose against the enzymes required to hydrolyse it to fermentable sugars | Phanerodontia chrysosporium |
| degradation | the partially purified LiP is able to degrade toxic synthetic polymer polyvinyl chloride (PVC) films, resulting in a 31% weight reduction of the films. LiP can effectively transform an endocrine disruptive hormone known as 17beta-estradiol (E2), which is considered a pollutant once released into the environment. Veratryl alcohol facilitates the enhanced removal and transformation of E2 by LiP and can perhaps also remove other closely related endocrine-disrupting impurities | Phanerodontia chrysosporium |
| additional information | lignin peroxidase has a broad spectrum of potential industrial and biotechnological applications attributed by its non-specific catalytic mechanism towards a variety of substrates. The use of LiP may provide a cost-effective, efficient and greener route for the transformation of biomass into second-generation (2 G) biofuels and other high-value green biochemicals, and thus effectively improve the economics of biorefineries. This biocatalyst can be applied in diverse industries such as pulp and paper mills, biofuels, food and feed, pharmaceuticals and also serve as a bioremediation agent, overview | Phanerodontia chrysosporium |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | the enzyme is secreted. Isozyme H8 is an extracellular globular glycoprotein | Phanerodontia chrysosporium | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 veratryl alcohol + H2O2 | Phanerodontia chrysosporium | - |
2 veratryl aldehyde + 2 H2O | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Phanerodontia chrysosporium | D1M7B6 | isozyme LiPH8; strains of Phanerochaete chrysosporium have multiple LiP-encoding genes and secrete the enzyme as numerous isozymes (H1, H2, H6, H7, H8 and H10) | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | isozyme H8 is an extracellular globular glycoprotein. The enzyme is N- and O-glycosylated to protect it against proteolytic degradation | Phanerodontia chrysosporium |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-dimethoxyphenyl)methanol radical + 2 H2O | catalytic mechanism of LiP on the oxidation of phenolic substrates (AH) and LiP is protected from suicidal inactivation by veratryl alcohol cation radicals | Phanerodontia chrysosporium |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 veratryl alcohol + H2O2 | - |
Phanerodontia chrysosporium | 2 veratryl aldehyde + 2 H2O | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| diarylpropane peroxidase | - |
Phanerodontia chrysosporium |
| ligninase I | - |
Phanerodontia chrysosporium |
| LIP | - |
Phanerodontia chrysosporium |
| LiPH8 | - |
Phanerodontia chrysosporium |
| microbial lignin peroxidase | - |
Phanerodontia chrysosporium |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
lignin peroxidases have low optimum pH of 3.0-4.5 and theoretical pIs of 3.3-4.7, depending on the isozyme | Phanerodontia chrysosporium |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| heme | the heme residue in LiP is embedded between the proximal and distal domains located in the interior part of the protein | Phanerodontia chrysosporium | |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Phanerodontia chrysosporium | lignin peroxidases have low optimum pH of 3.0-4.5 and theoretical pIs of 3.3-4.7, depending on the isozyme | - |
additional information |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | lignin peroxidases have a narrower heme access cavity than classical peroxidases, such as HRP and the low-redox potential fungal Coprinus cinerea peroxidase (CiP), which limits the interaction of the heme residue with some substrates and the oxidation thereof | Phanerodontia chrysosporium |
| physiological function | in native producers, LiP is secreted with veratryl alcohol (VA, 3,4-dimethoxybenzyl alcohol), a natural phenolic substrate of LiP that acts as a small diffusible redox mediator for the conversion of inaccessible substrates | Phanerodontia chrysosporium |
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