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
-
whitening
-
textile
-
anti-tyrosinase
- o-quinones
-
manganese-dependent
- l-3,4-dihydroxyphenylalanine
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microphthalmia-associated
-
anti-melanogenic
- o-diphenols
- bjerkandera
- arbutin
-
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
-
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
ECTree
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Engineering
Engineering on EC 1.11.1.14 - lignin peroxidase
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A140G/A243R/A317P
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kcat/Km for 2,4-dichlorophenol is 4fold higher than wild-type value, kcat/Km for H2O2 is 89fold higher than wild-type value
A140G/S190P/P193A/S196F/E208Q
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the variant shows increased 2,4-dichlorophenol degradation activity (ca. 1.6fold) and stability against H2O2. Kcat for H2O2 increases over the wild type value by about 6.5fold, the Km values for H2O2 is lower than wild type value
A55R/N156E/H239E
H102T/S119R/N120T/Q126K/A243R/A315G
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kcat/Km for 2,4-dichlorophenol is fold higher than wild-type value, kcat/Km for H2O2 is 89fold higher than wild-type value
P106R/Q210H/L211V/A243R/F255L
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kcat/Km for 2,4-dichlorophenol is 4fold higher than wild-type value, kcat/Km for H2O2 is 89fold higher than wild-type value
P106R/S119R/N120T/S228Y/A272G/L275V/A315G/A317T
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the variant shows increased 2,4-dichlorophenol degradation activity (ca. 1.6fold) and stability against H2O2. Kcat for H2O2 increases over the wild type value by about 6.5fold, the Km values for H2O2 is lower than wild type value
S274L/L275F/A292
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the variant shows increased 2,4-dichlorophenol degradation activity (ca. 1.6fold) and stability against H2O2. Kcat for H2O2 increases over the wild type value by about 6.5fold, the Km values for H2O2 is lower than wild type value
S49C/A67C/H239E
site-directed mutagenesis, improved thermostability of the synthetic LiPH8 variant (PDB ID 6ISS) capable of strengthening the helix-loop interactions under acidic conditions. The mutant retains excellent thermostability at pH 2.5 with a 10fold increase in t1/2 (2.52 h at 25°C) compared with that of the wild-type enzyme. The recombinant LiPH8 variant is the only unique lignin peroxidase containing five disulfide bridges, and the helix-loop interactions of the synthetic disulfide bridge and ionic salt bridge in its structure are responsible for stabilizing the Ca2+-binding region and heme environment, resulting in an increase in overall structural resistance against acidic conditions
additional information
site-directed mutagenesis the triple mutant of LiPH8 with 2 additional saltbridges on the solvent-exposed regions shows excellent stability and oxidation activity under extremely acidic conditions down to pH 2.6. The stabilized mutant shows higher activity levels at all three pH levels tested, as compared to wild-type, with the highest activity at pH 2.6. Increased conversion of lignin dimer, convertion of 96.1% and 45.3% of the dimer at pH 2.6 and pH 5.0, respectively
A55R/N156E/H239E
site-directed mutagenesis, a rationally designed variant, that demonstrates a 12.5fold increased half-life under extremely acidic conditions, 9.9fold increased catalytic efficiency toward veratryl alcohol, and a 7.8fold enhanced lignin model dimer conversion efficiency compared to those of native LiPH8. The mutant has two constructed salt bridges. See for structure: PDB ID 6A6Q. Introduction of strong ionic salt bridges based on computational design results in a LiPH8 variant with markedly improved stability, as well as higher activity under acidic pH conditions
design of active LiPH8 variants for increased stability in intensively acidic environments. Introduction of new strong salt bridges at effective locations and optimized interactions between charged residues and their environments are vital for active and stable LiP at acidic pH. Molecular dynamics (MD) simulation of the solvated structure under the desired conditions and calculating the Gibbs free energy of the variant are used for creating an acid-stable LiP variant, followed by protein X-ray crystallography
additional information
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design of active LiPH8 variants for increased stability in intensively acidic environments. Introduction of new strong salt bridges at effective locations and optimized interactions between charged residues and their environments are vital for active and stable LiP at acidic pH. Molecular dynamics (MD) simulation of the solvated structure under the desired conditions and calculating the Gibbs free energy of the variant are used for creating an acid-stable LiP variant, followed by protein X-ray crystallography
additional information
engineering of lignin peroxidase isozyme H8 and other enzymes involved in lignin depolymerization including targeting stability at low pH. Catalysis of degradation of the dimer to products by an acid-stabilized variant of lignin peroxidase isozyme H8 increases from 38.4% at pH 5.0 to 92.5% at pH 2.6. At pH 2.6, the observed product distribution results from 65.5% beta-O-4' ether bond cleavage, 27.0% Calpha-C1 carbon bond cleavage, and 3.6% Calpha-oxidation as by-product
additional information
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engineering of lignin peroxidase isozyme H8 and other enzymes involved in lignin depolymerization including targeting stability at low pH. Catalysis of degradation of the dimer to products by an acid-stabilized variant of lignin peroxidase isozyme H8 increases from 38.4% at pH 5.0 to 92.5% at pH 2.6. At pH 2.6, the observed product distribution results from 65.5% beta-O-4' ether bond cleavage, 27.0% Calpha-C1 carbon bond cleavage, and 3.6% Calpha-oxidation as by-product
additional information
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enzyme LiP obtained from a wild isolate of Phanerochaete chrysosporium immobilized on polyurethane foam cubes is purified 21fold using ammonium sulfate precipitation and size exclusion chromatography. The enzyme with a molecular mass of 55 kDa exhibited a considerably higher pH tolerance and thermostability compared with the native enzyme. It shows a strong affinity for the substrate veratryl alcohol and has kinetic constant values of 142.86 micromol and 0.065 mM. inhibited the activity, while ethanol, EDTA, Cu2+, Mn+, Na+, and Fe2+ exhibited induction. Purified LiP completely decolorizes (100%) bromophenyl blue, bromothymol blue, and bromocresol green. The 96% and 72% degradation obtained with phenol and Congo red is also higher compared to crude LiP. Treatment with LiP shows reduction in acid detergent lignin (ADL) as compared to untreated straws, with a maximum of 2.87 units obtained in jowar followed by 2.66 units in paddy straw. The digestibility of all straws increased, the response varying from a maximum of 21.27 units in proso millet to a minimum of 12.32 units obtained in little millet. The enzyme from immobilized organism exhibits an enhanced pH stability compared with the native enzyme obtained in the submerged cultures. It retains over 75% of activity at pH 6.5 for over 15 min
additional information
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fungal metabolites are playing an immense role in developing various sustainable waste treatment processes. Production and characterization of a fungal lignin peroxidase with a potential to degrade polyvinyl chloride, method optimization, overview
additional information
improving the thermostability of LiP in acidic environments is required for effective lignin depolymerization in practical applications
additional information
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fungal metabolites are playing an immense role in developing various sustainable waste treatment processes. Production and characterization of a fungal lignin peroxidase with a potential to degrade polyvinyl chloride, method optimization, overview
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additional information
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partially purified lignin peroxidase (LiP) from Pseudomonas fluorescens strain LiP-RL5 is immobilized on graphene oxide functionalized MnFe2O4 nanoparticles (10 nm, synthesized by sol-gel auto-combustion) to fabricate a new hyperactive and thermostable nanobiocatalyst, immobilization method evaluation, overview. Immobilized LiP is quite stable at 50°C with the half-life of 14 h and shows higher tolerance towards various metal ions and solvents than free LiP. Immobilized LiP retains 50% of enzyme activity even after nine consecutive runs. When tested against various textile dyes, the immobilized LiP is effective with higher dye decolourization efficiency (up to 88%) within 1 h of incubation at 30°C
additional information
Pseudomonas fluorescens LiP-RL5
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partially purified lignin peroxidase (LiP) from Pseudomonas fluorescens strain LiP-RL5 is immobilized on graphene oxide functionalized MnFe2O4 nanoparticles (10 nm, synthesized by sol-gel auto-combustion) to fabricate a new hyperactive and thermostable nanobiocatalyst, immobilization method evaluation, overview. Immobilized LiP is quite stable at 50°C with the half-life of 14 h and shows higher tolerance towards various metal ions and solvents than free LiP. Immobilized LiP retains 50% of enzyme activity even after nine consecutive runs. When tested against various textile dyes, the immobilized LiP is effective with higher dye decolourization efficiency (up to 88%) within 1 h of incubation at 30°C
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