1.11.1.14: lignin peroxidase
This is an abbreviated version!
For detailed information about lignin peroxidase, go to the full flat file.
Word Map on EC 1.11.1.14
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1.11.1.14
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chrysosporium
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phanerochaete
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manganese
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laccase
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melanin
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ligninolytic
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veratryl
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peroxidases
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melanoma
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melanogenesis
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white-rot
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kojic
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decolor
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l-dopa
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diphenolase
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basidiomycete
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trametes
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monophenolase
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versicolor
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hyperpigmentation
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lignin-degrading
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whitening
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textile
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anti-tyrosinase
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o-quinones
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manganese-dependent
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l-3,4-dihydroxyphenylalanine
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microphthalmia-associated
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anti-melanogenic
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o-diphenols
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bjerkandera
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arbutin
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skin-whitening
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non-phenolic
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1.14.18.1
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dopaquinone
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phlebia
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tyrosinase-related
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delignification
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dopachrome
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remazol
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lignocellulolytic
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anti-melanogenesis
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eryngii
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tyrosinases
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catecholase
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depigmenting
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biotechnology
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dye-decolorizing
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synthesis
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environmental protection
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lignocellulose-degrading
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analysis
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degradation
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industry
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irpex
- 1.11.1.14
- chrysosporium
- phanerochaete
- manganese
- laccase
- melanin
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ligninolytic
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veratryl
- peroxidases
- melanoma
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melanogenesis
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white-rot
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kojic
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decolor
- l-dopa
- diphenolase
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basidiomycete
- trametes
- monophenolase
- versicolor
- hyperpigmentation
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lignin-degrading
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whitening
-
textile
-
anti-tyrosinase
- o-quinones
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manganese-dependent
- l-3,4-dihydroxyphenylalanine
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microphthalmia-associated
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anti-melanogenic
- o-diphenols
- bjerkandera
- arbutin
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skin-whitening
-
non-phenolic
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1.14.18.1
- dopaquinone
- phlebia
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tyrosinase-related
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delignification
- dopachrome
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remazol
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lignocellulolytic
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anti-melanogenesis
- eryngii
- tyrosinases
- catecholase
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depigmenting
- biotechnology
-
dye-decolorizing
- synthesis
- environmental protection
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lignocellulose-degrading
- analysis
- degradation
- industry
- irpex
Reaction
Synonyms
ALiP-P3, bacterial lignin peroxidase, diarylpropane oxygenase, diarylpropane peroxidase, diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving), DypB, fungal lignin peroxidase, Glg4, H2O2-dependent ligninase, heme-containing lignin peroxidase, heme-containing peroxidase, lignin peroxidase, lignin peroxidase H8, lignin peroxidase isozyme H8, lignin peroxidase LIII, ligninase, ligninase H2, ligninase H8, ligninase I, ligninase LG5, LIP, Lip1, LIP2, LiPH8, lipJ, LPA, LPOA, microbial lignin peroxidase, More, mushroom tyrosinase, oxygenase, diarylpropane, Pr-lip1, Pr-lip4
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General Information
General Information on EC 1.11.1.14 - lignin peroxidase
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evolution
physiological function
additional information
evolution of MnPs (EC 1.11.1.13) into LiPs (EC 1.11.1.1.14) parallels the removal of Mn2+ binding sites and the creation of surface tryptophan residues, which accelerates interaction with the bulky structure and oxidation of high-redox-potential substrates, such as lignin. Note that this evolution might unexpectedly result in poor acid stability of the modern LiP. Various white-rot fungi, such as Phanerochaete chrysosporium, Trametes sp., Coriolopsis byrsina, Phellinus rimosus, and Lentinus sp. possess LiP isozymes which are not stable under extremely acidic conditions (e.g. pH values lower than pH 3.0). Even though LiPs and MnPs share a similar overall structure, as both belong to members of the peroxidase family, MnPs found in fungi, such as Ceriporiopsis subvermispora and Pleurotus ostreatus, exhibit relatively higher stability under acidic pH conditions. The considerable acid stability observed could be a result of several noncovalent interactions, such as salt bridges and hydrogen bonding networks
evolution
isozyme lignin peroxidase A, LPA, is the major isozyme of the LP H8 family
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LiP shows lignin degrading and coal depolymerization activity
physiological function
wild-type Rhodococcus jostii RHA1 shows hydrogen peroxide-dependent activity, whereas the DypB knockout strain shows no observable activity in the presence or absence of hydrogen peroxide and a significant decrease in activity compared to that of the wild-type strain
physiological function
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the promiscuous activity of tyrosinase not only oxidizes veratryl alcohol, a commonly used nonphenolic substrate for assaying ligninolytic activity, to veratraldehyde but also cleaves the 4-O-5 and Calpha-Cbeta bonds in 4-phenoxyphenol and guaiacyl glycerol-beta-guaiacyl ether (GGE) that are dimeric lignin model compounds. The promiscuous activity oxidizes lignin-related high redox potential substrates
physiological function
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extracellular enzymes of white-rot fungi play an important role in the deconstruction of lignin in lignocellulosic biomass. Lignin peroxidase plays a role in biodegradation of plant cell wall lignin. LiP may also play a major role in the bio-delignification of lignocellulose in crop residues. Lignin peroxidase is an extracellular hemeprotein that is H2O2-dependent, with an unusually high redox potential and low optimum pH. It is capable of oxidizing a variety of reducing substrates, including polymeric substrates
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
physiological function
lignin peroxidases catalyze a variety of reactions, resulting in cleavage of both beta-O-4' ether bonds and C-C bonds in lignin, both of which are essential for depolymerizing lignin into fragments amendable to biological or chemical upgrading to valuable products. The pH is a key driving force for selective and efficient lignin peroxidase isozyme H8 catalyzed depolymerization of the phenolic lignin dimer
physiological function
peroxidases are considered essential agents of lignin degradation by white-rot basidiomycetes. Low-molecularweight oxidants likely have a primary role in lignin breakdown because many of these fungi delignify wood before its porosity has sufficiently increased for enzymes to infiltrate. It has been proposed that lignin peroxidases fulfill this role by oxidizing the secreted fungal metabolite veratryl alcohol to its aryl cation radical, releasing it to act as a one-electron lignin oxidant within woody plant cell walls, but the fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant. Isozyme LPA releases insignificant quantities of VA cation radical, and a different mechanism produces small ligninolytic oxidants during white rot
physiological function
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Phanerochaete chrysosporium strain NK-1 is able to use polyvinyl chloride (PVC) as the sole source of carbon and energy, and this degradation of the polymer is mainly facilitated by the production of peroxidases. Thus, the enzyme production is considered as the function of cellular growth. Extracellular lignin peroxidases from Phanerocheate chrysosporium play a significant role in the degradation of complex polymeric compounds like PVC
physiological function
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synergistic effect of lignin peroxidase and cellulase in Aspergillus oryzae solid-state fermentation substrate on enzyme-catalyzed oxidative degradation of lignin. beta-Glucosidase is the key enzyme that inhibits the oxidative degradation of lignin. The results lay the foundation for screening and optimizing fermentation process conditions of the LiP strain, and improving the efficiency of enzyme-catalyzed oxidative degradation of lignin
physiological function
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the enzyme catalyzes decolorization in the presence or in the absence of the mediator veratryl alcohol
physiological function
Aspergillus oryzae CGMCC5992
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synergistic effect of lignin peroxidase and cellulase in Aspergillus oryzae solid-state fermentation substrate on enzyme-catalyzed oxidative degradation of lignin. beta-Glucosidase is the key enzyme that inhibits the oxidative degradation of lignin. The results lay the foundation for screening and optimizing fermentation process conditions of the LiP strain, and improving the efficiency of enzyme-catalyzed oxidative degradation of lignin
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physiological function
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LiP shows lignin degrading and coal depolymerization activity
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physiological function
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the enzyme catalyzes decolorization in the presence or in the absence of the mediator veratryl alcohol
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physiological function
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Phanerochaete chrysosporium strain NK-1 is able to use polyvinyl chloride (PVC) as the sole source of carbon and energy, and this degradation of the polymer is mainly facilitated by the production of peroxidases. Thus, the enzyme production is considered as the function of cellular growth. Extracellular lignin peroxidases from Phanerocheate chrysosporium play a significant role in the degradation of complex polymeric compounds like PVC
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lignin peroxidase is unable to degrade atrazine, analysis of the connection between the structural and dynamical properties of the enzyme and its incapability to degrade atrazine, protein-ligand docking and molecular dynamics study, three-dimensional modeling of the lignin peroxidase-atrazine complex, overview. Atrazine has no access to heme edge due to the electric charges of the delocalized S-triazine ring. The detected phenomenon suggests that the small size of the ligands only is not a sufficient condition to access the active site. Their physicochemical properties also influence the structural behaviour of the channel. The lignin peroxidase can directly oxidize lignin in the partially degraded plant cell walls cannot be excluded. Lignin peroxidase has a so-called ligand access channel which allows direct interaction between the substrate and the heme. Residues His82, Ile85, Glu146, Phe148, Asp183, Val184 and Gln222 are located in this channel. The channel is sterically restricted and does not allow access to large bulky (lignin) substrates. The enzyme's natural substrate, veratrol, can easily approach heme through the ligand access channel. Based on the results of protein-ligand docking, atrazine can find an energetically favourable position in the environment of the ligand channel residues, although, the mathematical probability of the formation of these complexes is not significant (10%, 16% and 53% frequency values at three different temperatures)
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