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Information on EC 1.11.1.14 - lignin peroxidase and Organism(s) Phanerodontia chrysosporium and UniProt Accession P49012

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EC Tree
     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.14 lignin peroxidase
IUBMB Comments
A hemoprotein, involved in the oxidative breakdown of lignin by white-rot basidiomycete fungi. The reaction involves an initial oxidation of the heme iron by hydrogen peroxide, forming compound I (FeIV=O radical cation) at the active site. A single one-electron reduction of compound I by an electron derived from a substrate molecule yields compound II (FeIV=O non-radical cation), followed by a second one-electron transfer that returns the enzyme to the ferric oxidation state. The electron transfer events convert the substrate molecule into a transient cation radical intermediate that fragments spontaneously. The enzyme can act on a wide range of aromatic compounds, including methoxybenzenes and nonphenolic beta-O-4 linked arylglycerol beta-aryl ethers, but cannot act directly on the lignin molecule, which is too large to fit into the active site. However larger lignin molecules can be degraded in the presence of veratryl alcohol. It has been suggested that the free radical that is formed when the enzyme acts on veratryl alcohol can diffuse into the lignified cell wall, where it oxidizes lignin and other organic substrates. In the presence of high concentration of hydrogen peroxide and lack of substrate, the enzyme forms a catalytically inactive form (compound III). This form can be rescued by interaction with two molecules of the free radical products. In the case of veratryl alcohol, such an interaction yields two molecules of veratryl aldehyde.
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Phanerodontia chrysosporium
UNIPROT: P49012
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Word Map
The taxonomic range for the selected organisms is: Phanerodontia chrysosporium
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
lignin peroxidase, mushroom tyrosinase, ligninase, liph8, heme-containing peroxidase, lignin peroxidase isozyme h8, diarylpropane oxygenase, ligninase h8, alip-p3, lignin peroxidase h8, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diarylpropane oxygenase
-
-
-
-
diarylpropane peroxidase
diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving)
-
-
-
-
fungal lignin peroxidase
H2O2-dependent ligninase
-
-
heme-containing lignin peroxidase
-
-
heme-containing peroxidase
-
-
lignin peroxidase
lignin peroxidase H8
-
lignin peroxidase isozyme H8
-
ligninase H8
ligninase I
LiPH8
microbial lignin peroxidase
-
oxygenase, diarylpropane
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-dimethoxyphenyl)methanol radical + 2 H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol:hydrogen-peroxide oxidoreductase
A hemoprotein, involved in the oxidative breakdown of lignin by white-rot basidiomycete fungi. The reaction involves an initial oxidation of the heme iron by hydrogen peroxide, forming compound I (FeIV=O radical cation) at the active site. A single one-electron reduction of compound I by an electron derived from a substrate molecule yields compound II (FeIV=O non-radical cation), followed by a second one-electron transfer that returns the enzyme to the ferric oxidation state. The electron transfer events convert the substrate molecule into a transient cation radical intermediate that fragments spontaneously. The enzyme can act on a wide range of aromatic compounds, including methoxybenzenes and nonphenolic beta-O-4 linked arylglycerol beta-aryl ethers, but cannot act directly on the lignin molecule, which is too large to fit into the active site. However larger lignin molecules can be degraded in the presence of veratryl alcohol. It has been suggested that the free radical that is formed when the enzyme acts on veratryl alcohol can diffuse into the lignified cell wall, where it oxidizes lignin and other organic substrates. In the presence of high concentration of hydrogen peroxide and lack of substrate, the enzyme forms a catalytically inactive form (compound III). This form can be rescued by interaction with two molecules of the free radical products. In the case of veratryl alcohol, such an interaction yields two molecules of veratryl aldehyde.
CAS REGISTRY NUMBER
COMMENTARY hide
93792-13-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Reactive Black 5 + H2O2
?
show the reaction diagram
lignin peroxidase can only oxidize Reactive Black 5 in the presence of redox mediators such as veratryl alcohol
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
show the reaction diagram
-
-
-
?
1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol + H2O2
3,4-dimethoxybenzaldehyde + 1-(3,4-dimethyl-phenyl)ethane-1,2-diol + H2O
show the reaction diagram
-
-
-
-
?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxy-phenyl)propane + O2 + H2O2
1-(4'-methoxyphenyl)-1,2-dihydroxyethane + 3,4-diethoxybenzaldehyde
show the reaction diagram
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
show the reaction diagram
1-(4-ethoxy-3-methoxyphenyl)-1,2-propene + O2 + H2O2
1-(4-ethoxy-3-methoxyphenyl)-1,2-dihydroxypropane
show the reaction diagram
1-(4-ethoxy-3-methoxyphenyl)propane + O2 + H2O2
1-(4-ethoxy-3-methoxyphenyl)1-hydroxypropane
show the reaction diagram
-
-
-
?
2 veratryl alcohol + H2O2
2 veratryl aldehyde + 2 H2O
show the reaction diagram
2,4-dichlorophenol + H2O2
?
show the reaction diagram
-
-
-
-
?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
show the reaction diagram
4,5-dichlorocatechol + H2O2
?
show the reaction diagram
-
50 mM sodium tartrate buffer, pH 3.5 at 25°C, hydrogen peroxide concentration is 1 mM, addition of gelatin to the reaction mixtures protected lignin peroxidase from precipitation
formation of water-insoluble oxidation products
-
?
4-chlorocatechol + H2O2
?
show the reaction diagram
-
50 mM sodium tartrate buffer, pH 3.5 at 25°C, hydrogen peroxide concentration is 1 mM, addition of gelatin to the reaction mixtures protected lignin peroxidase from precipitation
formation of water-insoluble oxidation products
-
?
4-methoxymandelic acid + veratryl alcohol
?
show the reaction diagram
-
-
-
?
4-methylcatechol + H2O2
?
show the reaction diagram
-
50 mM sodium tartrate buffer, pH 3.5 at 25°C, hydrogen peroxide concentration is 3 mM, addition of gelatin to the reaction mixtures protected lignin peroxidase from precipitation
formation of water-insoluble oxidation products
-
?
4-methylthio-2-oxobutanoate + H2O2
?
show the reaction diagram
-
only in presence of veratryl alcohol, it possibly reacts with a veratryl alcohol radical to produce ethylene
-
-
?
catechol + H2O2
?
show the reaction diagram
-
50 mM sodium tartrate buffer, pH 3.5 at 25°C, hydrogen peroxide concentration is 2 mM, addition of gelatin to the reaction mixtures protected lignin peroxidase from precipitation
formation of water-insoluble oxidation products
-
?
catechol + H2O2
? + 2 H2O
show the reaction diagram
-
-
-
-
?
dimethoxyphenol + H2O2
? + 2 H2O
show the reaction diagram
-
-
-
-
?
fuchsine + H2O2
?
show the reaction diagram
-
-
-
-
?
guaiacol + H2O2
? + 2 H2O
show the reaction diagram
-
-
-
-
?
melanin + H2O2
?
show the reaction diagram
-
pH 3, 40 °C, 15 IU/ml, and 10 h incubation are the optimal conditions for the degradation of the melanin. The use of the mediator veratryl alcohol is effective to enhance the efficacy of the melanin degradation, with up to 92% decolorization, method evaluation and optimization, overview
-
-
?
mitoxantrone + H2O2
hexahydronaphtho-[2,3-f]-quinoxaline-7,12-dione + H2O
show the reaction diagram
-
low efficiency
-
-
?
non-phenolic substrates + H2O2
?
show the reaction diagram
-
e.g. 1,2,4-trimethoxybenzene, 4,4'-dimethoxybiphenyl, isoeugenol methylether, 1-(3,4-dimethoxyphenyl)-2-(2, 4-dichlorophenoxyl)-ethanol, guaiacyl glycerolether
-
-
?
oxytetracycline + H2O2
?
show the reaction diagram
-
LiP shows strong degrading ability
-
-
?
pyrogallol red + H2O2
?
show the reaction diagram
-
-
-
-
?
rhodamine B + H2O2
?
show the reaction diagram
-
-
-
-
?
syringaldehyde + H2O2
? + 2 H2O
show the reaction diagram
-
-
-
-
?
tetracycline + H2O2
?
show the reaction diagram
-
LiP shows strong degrading ability
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
show the reaction diagram
veratryl alcohol + H2O2
?
show the reaction diagram
-
-
-
-
?
veratryl alcohol + H2O2
veratraldehyde + H2O
show the reaction diagram
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
show the reaction diagram
xylene cyanol + H2O2
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
show the reaction diagram
2 veratryl alcohol + H2O2
2 veratryl aldehyde + 2 H2O
show the reaction diagram
veratryl alcohol + H2O2
veratraldehyde + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
Mg2+ and Ca2+ fail to have any effect on the LiP activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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-
3-Amino-1,2,4-triazole
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cetyltrimethylammonium bromide
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weak
Silver nitrate
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sodium bis (2-ethylhexyl)-sulfosuccinate
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a mixed reversed micelle formed by anionic surfactant sodium bis (2-ethylhexyl)-sulfosuccinate and non-ionic surfactant polyoxyethylene lauryl ether (Brij30) is used to increase the catalytic activity
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
H2O2
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degradation of tetracycline and oxytetracycline is not detected without the addition of H2O2, but enhances greatly with the addition of 0.1 mM H2O2
veratryl alcohol
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.163 - 0.79
2,4-Dichlorophenol
0.009 - 23.6
H2O2
1.57
Mn2+
-
mutant enzyme
0.055 - 3.54
veratryl alcohol
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
37.1 - 333.3
2,4-Dichlorophenol
10.83 - 176.7
H2O2
13.72
veratryl alcohol
-
pH 6.5, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.88
veratryl alcohol
-
pH 6.5, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11.4
-
1,2-bis(3,4-di-methoxyphenyl)propane-1,3-diol
15.9
-
pH 3.0 tartrate buffer, 30°C
20.3
-
pH 3.0 tartrate buffer, 30°C
8.4
-
veratryl alcohol
8.48
-
isozyme III
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5
substrate veratryl alcohol, 25°C
3.6
-
catalytic activity of lignin peroxidase in sodium bis(2-ethylhexyl)sulfosuccinate /isooctane/toluene/water reverse micelles
4.2
-
optimum pH for tetracycline and oxytetracycline degradation
4.8
-
in the AOT/Brij30 mixed reversed micelles. The optimum pH occurres at ca. 4.8, which is higher than that in a single AOT reversed micelle
5.5
-
purified enzyme from immobilized Phanerochaete chrysosporium, with veratryl alcohol as the substrate
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 6
-
activity range
2.8 - 5.4
-
pH range for tetracycline and oxytetracycline degradation, no removal is observed when pH was below 2.8 or above 5.4. The degradation percentage is comparatively stable and high when pH is between 3.6 and 4.2 for tetracycline and oxytetracycline
3 - 10
-
activity range, purified enzyme from immobilized Phanerochaete chrysosporium, profile overview
3 - 9
-
activity range, optimal activity at pH 5.0, almost inactive at pH 11.0
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
45
substrate veratryl alcohol, pH 3.5
45 - 60
substrate veratryl alcohol, pH 4.5
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 30
-
enzyme activity increases as the temperature increases from 10°C to 30°C in vivo. Further increase in temperature results in an obvious decrease in the amount of enzyme production by the fungal strain
20 - 40
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at 30°C, tetracycline is nearly totally removed and this degradation percentage keeps unchanged until 37°C, whereas the degradation of oxytetracycline reaches about 90% at 30°C and increases with temperature until it is 37°C. At 20°C, the degradation of tetracycline reaches about 78%, the value for oxytetracycline is 83%. When temperature exceeds 37°C, the degradation of both tetracycline and oxytetracycline decreases
20 - 60
-
activity range
25 - 40
-
over 50% of maximal activity within this range, profile overview
25 - 75
-
pH 5, 100% lignin peroxidase activity is retained at 55°C after incubation. The lignin peroxidase activity drops more than 75% at temperatures below 35°C and loses about 66% of its activity at a temperature of 75°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3
isoelectric focusing
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
the isolated sample from waste and contaminated soli is grown on a seaboard dextrose agar medium. Four different fungal colonies, named as Nk-1, Nk-2, Nk-3, and Nk-4, are isolated and purified from the sample. The maximum enzyme production occurs at a temperature 25°C, pH 5.0 in the 4th week of the incubation period with fungal strain, optimization of enzyme production method, overview. Phanerochaete chrysosporium strain NK-1 is able to use PVC as the sole source of carbon and energy
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LIG2_PHACH
371
0
39329
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39000
-
x * 39000, isozyme I, SDS-PAGE
41000
-
x * 41000, isozyme II, SDS-PAGE
42000
-
x * 42000, SDS-PAGE
43000
-
x * 43000, isozyme III, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isozyme H8 and W171 mutant
-
purified enzyme, hanging drop vapor diffusion method, mixing of 0.001 ml of 8 mg/ml protein solution in 10 mM succinate buffer, pH 6.0, with 0.001 ml of reservoir solution containing 16% PEG 6000, and equilibration of the mixture against 0.5 ml of reservoir solution, 7 days at 20°C, X-ray diffraction structure determination and analysis at 1.67 A resolution, modeling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A140G/A243R/A317P
-
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
-
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
-
kcat/Km for 2,4-dichlorophenol is fold higher than wild-type value, kcat/Km for H2O2 is 89fold higher than wild-type value
N182D/D183K/A36E
-
generating a Mn2+-binding site
P106R/Q210H/L211V/A243R/F255L
-
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
-
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
-
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
W171F
-
no activity towards veratryl alcohol
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
-
rapid inactivation
394601
3 - 11
-
the lignin peroxidase activity is stable at pH 5, lower at a low pH of 3 and is high below pH 7, more than 70% of activity is lost at pH 7-11
704959
6.5
-
immobilized enzyme, retains over 75% of activity at pH 6.5 for over 15 min
764314
additional information
-
lignin peroxidase is very stable over a broad range of pH
764590
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
-
retains nearly 30% of initial activity after 18 h, in presence of veratryl alcohol
25 - 75
-
pH 5, 100% lignin peroxidase activity is retained at 55°C after incubation. The lignin peroxidase activity drops more than 75% at temperatures below 35°C and loses about 66% of its activity at a temperature of 75°C
40
21 h, pH 4.0-6.5, 80% residual activity
45
-
after 2 h incubation at 45°C, 55% of the initial activity of the immobilized lignin peroxidase (on nanoporous gold) is still retained while the free lignin peroxidase is completely deactivated, pH 3.5 citrate buffer
50
stable for 48 h up to 50°C
60
6 h, complete loss of activity
60 - 80
-
the purified enzyme exhibits a higher thermostability and retains over 50% of the activity, even after 120 min of incubation at both 60°C and 65°C. Loss of 25% of the activitiy after 120 min at 70°C. 25% activity is maintained after 100 min at both 75°C and 80°C and activity is completely lost after 120 min
70
min, complete loss of activity
additional information
an extra disulfide and ionic salt bridge improves the thermostability of lignin peroxidase H8 under acidic condition. Native LiP under mild conditions with half-life (t1/2) of 8.2 days at pH 6.0 exhibits a marked decline in thermostability under acidic conditions with t1/2 of only 14 min at pH 2.5
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
high protein concentrations stabilize
-
lignin peroxidase in sodium bis(2-ethylhexyl)sulfosuccinate/isooctane/toluene/water reverse micelles reverse micelles shoes a the half-life of circa 12 h. under optimal conditions, at a molar ratio of water to sodium bis(2-ethylhexyl)sulfosuccinate of 11, pH 3.6, and a volume ratio of isooctane to toluene of 7–9
-
lyophilization, stable to
-
The results for the tests of the stability of lignin peroxidase show that the activity is more than 80% of the maximum for the first 12 h of incubation at an optimum pH of 5 and temperature of 55°C.
-
veratryl alcohol stabilizes at pH 3.5 and 23°C, lag-phases are not observed
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
-
acetone largely denatures lignin peroxidase
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-196°C, indefinitely stable
-
-20°C, stable as lyophilized powder
-
at 4°C the activity of the immobilized lignin peroxidase decreases slowly. After 1 month, about 95% activity is still retained, free lignin peroxidase loses about 30% of its initial activity, indicating that the storage stability of lignin peroxidase considerably increases after the immobilization on nanoporous gold
-
frozen, in crude concentrates of growth medium complete loss of activity within a month
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3 isozymes by ion-exchange chromatography
-
active solubilized recombinant enzyme expressed from Escherichia coli strain W3110 is purified by anion exchange chromatography using a 0-300 mM NaCl gradient (20 min, 2 ml/min flow rate) in 10 mM sodium tartrate, pH 5.5, containing 1 mM CaCl2
extracellular enzyme partially from strain NK-1 by ammonium sulfate fractionation and gel filtration
-
native extracellular enzyme 21fold by immobilization on polyurethane foam cubes, ammonium sulfate fractionation, ultrafiltration, and gel filtration
-
salt precipitation with 60% (NH4)2SO4, desalting column, Q FF ion exchange column and Sepharyl S-300 HR gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme cloning from strain NK-1, phylogenetic analysis
-
expression in Saccharomyces cerevisiae
-
gene LPOA, recombinant expression of the codon-optimized gene in Escherichia coli strain W3110. The cloned expression vector pFLAG1 and the resulting plasmid pFLAG1-Y00262 are directly used for expression, Escherichia coli strain DH5x02alpha is used for plasmid propagation. The apoenzyme accumulates in inclusion bodies
overexpression of isozyme H8 and W171 mutant in Escherichia coli
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant apoenzyme from inclusion bodies after expression in Escherichia coli strain W3110 by solubilization with 8 M urea. Subsequent in vitro refolding of the enzyme LP is performed using 2.1 M urea, 5 mM Ca2+, 0.01 mM hemin, 0.7 mM oxidized glutathione, 0.1 mM dithiothreitol, and 0.2 mg/ml protein, at pH 8.0
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
different mechanisms for the bioelectrocatalysis of the enzyme depend on the chemical nature of the mediators and are of a special interest both for fundamental science and for application of the enzyme as solid-phase bio(electro)catalyst for decomposition/detection of of recalcitrant aromatic compounds
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
degradation
environmental protection
industry
-
the enzyme can be used as biocatalytic in delignification (which is emerging owing to its superior selectivity, low energy consumption, and unparalleled sustainability) iIn the biorefinery utilizing lignocellulosic biomasses, lignin decomposition to value-added phenolic derivatives
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Paszczynski, A.; Huynh, V.B.; Crawford, R.L.
Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium
Arch. Biochem. Biophys.
244
750-765
1986
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F-1767
Manually annotated by BRENDA team
Tien, M.; Kirk, T.K.
Lignin-degrading enzyme from Phanerochaete chrysosporium: Purification, characterization, and catalytic properties of a unique H2O2-requiring oxygenase
Proc. Natl. Acad. Sci. USA
81
2280-2284
1984
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F-1767
Manually annotated by BRENDA team
Renganathan, V.; Miki, K.; Gold, M.H.
Multiple molecular forms of diarylpropane oxygenase, an H2O2-requiring, lignin-degrading enzyme from Phanerochaete chrysosporium
Arch. Biochem. Biophys.
241
304-314
1985
Phanerodontia chrysosporium
Manually annotated by BRENDA team
Andersson, L.A.; Renganathan, V.; Chiu, A.A.; Loehr, T.M.; Gold, M.H.
Spectral characterization of diarylpropane oxygenase, a novel peroxide-dependent, lignin-degrading heme enzyme
J. Biol. Chem.
260
6080-6087
1985
Phanerodontia chrysosporium
Manually annotated by BRENDA team
Gold, M.H.; Kuwahara, M.; Chiu, A.A.; Glenn, J.K.
Purification and characterization of an extracellular H2O2-requiring diarylpropane oxygenase from the white rot basidiomycete, Phanerochaete chrysosporium
Arch. Biochem. Biophys.
234
353-362
1984
Phanerodontia chrysosporium
Manually annotated by BRENDA team
Aitken, M.; Irvine, R.L.
Stability testing of ligninase and Mn-peroxidase from Phanerochaete chrysosporium
Biotechnol. Bioeng.
34
1251-1260
1989
Phanerodontia chrysosporium, Phanerodontia chrysosporium VKM F-1767
Manually annotated by BRENDA team
Khindaria, A.; Nie, G.; Aust, S.D.
Detection and characterization of the lignin peroxidase compound II-veratryl alcohol cation radical complex
Biochemistry
36
14181-14185
1997
Phanerodontia chrysosporium
Manually annotated by BRENDA team
Blodig, W.; Smith, A.T.; Doyle, W.A.; Piontek, K.
Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171. Implications for the reaction mechanism
J. Mol. Biol.
305
851-861
2001
Phanerodontia chrysosporium
Manually annotated by BRENDA team
Mester, T.; Tien, M.
Engineering of a manganese-binding site in lignin peroxidase isozyme H8 from Phanerochaete chrysosporium
Biochem. Biophys. Res. Commun.
284
723-728
2001
Phanerodontia chrysosporium
Manually annotated by BRENDA team
Liu, A.; Huang, X.; Song, S.; Wang, D.; Lu, X.; Qu, Y.; Gao, P.
Kinetics of the H2O2-dependent ligninase-catalyzed oxidation of veratryl alcohol in the presence of cationic surfactant studied by spectrophotometric technique
Spectrochim. Acta A
59
2547-2551
2003
Phanerodontia chrysosporium
Manually annotated by BRENDA team
Zhang, W.; Huang, X.; Li, Y.; Qu, Y.; Gao, P.
Catalytic activity of lignin peroxidase and partition of veratryl alcohol in AOT/isooctane/toluene/water reverse micelles
Appl. Microbiol. Biotechnol.
70
315-320
2006
Phanerodontia chrysosporium
Manually annotated by BRENDA team
Ferapontova, E.E.; Castillo, J.; Gorton, L.
Bioelectrocatalytic properties of lignin peroxidase from Phanerochaete chrysosporium in reactions with phenols, catechols and lignin-model compounds
Biochim. Biophys. Acta
1760
1343-1354
2006
Phanerodontia chrysosporium
Manually annotated by BRENDA team
Lan, J.; Huang, X.; Hu, M.; Li, Y.; Qu, Y.; Gao, P.; Wu, D.
High efficient degradation of dyes with lignin peroxidase coupled with glucose oxidase
J. Biotechnol.
123
483-490
2006
Phanerodontia chrysosporium
Manually annotated by BRENDA team
Pointing, S.B.; Pelling, A.L.; Smith, G.J.; Hyde, K.D.; Reddy, C.A.
Screening of basidiomycetes and xylariaceous fungi for lignin peroxidase and laccase gene-specific sequences
Mycol. Res.
109
115-124
2005
Trametes versicolor, Trametes coccinea, Trametes sanguinea, Panus sp., Perenniporia medulla-panis, Phanerodontia chrysosporium (P06181), Phanerodontia chrysosporium (P11543), Phanerodontia chrysosporium (Q9UW80), Phanerodontia chrysosporium H10 (P11543), Phanerodontia chrysosporium H2 (Q9UW80), Phanerodontia chrysosporium H8 (P06181)
Manually annotated by BRENDA team
Zhang, Y.; Huang, X.R.; Huang, F.; Li, Y.Z.; Qu, Y.B.; Gao, P.J.
Catalytic performance of lignin peroxidase in a novel reverse micelle
Colloids Surf. B Biointerfaces
65
50-53
2008
Phanerodontia chrysosporium
Manually annotated by BRENDA team
Ryu, K.; Hwang, S.Y.; Kim, K.H.; Kang, J.H.; Lee, E.K.
Functionality improvement of fungal lignin peroxidase by DNA shuffling for 2,4-dichlorophenol degradability and H2O2 stability
J. Biotechnol.
133
110-115
2008
Phanerodontia chrysosporium
Manually annotated by BRENDA team
Ryu, K.; Kang, J.H.; Wang, L.; Lee, E.K.
Expression in yeast of secreted lignin peroxidase with improved 2,4-dichlorophenol degradability by DNA shuffling
J. Biotechnol.
135
241-246
2008
Phanerodontia chrysosporium
Manually annotated by BRENDA team
Alam, M.Z.; Mansor, M.F.; Jalal, K.C.
Optimization of decolorization of methylene blue by lignin peroxidase enzyme produced from sewage sludge with Phanerocheate chrysosporium
J. Hazard. Mater.
162
708-715
2009
Phanerodontia chrysosporium
Manually annotated by BRENDA team
Cohen, S.; Belinky, P.A.; Hadar, Y.; Dosoretz, C.G.
Characterization of catechol derivative removal by lignin peroxidase in aqueous mixture
Biores. Technol.
100
2247-2253
2009
Phanerodontia chrysosporium
Manually annotated by BRENDA team
Qiu, H.; Li, Y.; Ji, G.; Zhou, G.; Huang, X.; Qu, Y.; Gao, P.
Immobilization of lignin peroxidase on nanoporous gold: enzymatic properties and in situ release of H2O2 by co-immobilized glucose oxidase
Biores. Technol.
100
3837-3842
2009
Phanerodontia chrysosporium
Manually annotated by BRENDA team
Sharma, J.; Yadav, R.; Singh, N.; Yadav, K.
Secretion and characterisation of ligninperoxidases by some new indigenous lignolytic fungi
Biosci. Biotechnol. Res. Asia
5
673-678
2008
Agaricus campestris, Phanerodontia chrysosporium, Trametes hirsuta, Trametes versicolor, Pleurotus ostreatus, Lentinus sajor-caju, Volvariella volvacea, Tropicoporus linteus, Polyporous velutinus, Trametes elegans, Pleurotus sapidus, Lentinus sajor-caju MTCC 141, Trametes hirsuta MTCC 136, Pleurotus ostreatus MTCC 1803, Trametes versicolor MTCC 138, Pleurotus sapidus MTCC 1807, Volvariella volvacea MTCC 957, Polyporous velutinus MTCC 1813, Trametes elegans MTCC 1812, Agaricus campestris MTCC 972, Tropicoporus linteus MTCC 1175, Phanerodontia chrysosporium MTCC 787
-
Manually annotated by BRENDA team
Lan, J.; Zhang, Y.; Huang, X.; Hu, M.; Liu, W.; Li, Y.; Qu, Y.; Gao, P.
Improvement of the catalytic performance of lignin peroxidase in reversed micelles
J. Chem. Technol. Biotechnol.
83
64-70
2008
Phanerodontia chrysosporium, Phanerodontia chrysosporium F. F. Lombard / ME-446 / ATCC 43541
-
Manually annotated by BRENDA team
Ruiz-Duenas, F.J.; Morales, M.; Garcia, E.; Miki, Y.; Martinez, M.J.; Martinez, A.T.
Substrate oxidation sites in versatile peroxidase and other basidiomycete peroxidases
J. Exp. Bot.
60
441-452
2009
Phanerodontia chrysosporium (P49012)
Manually annotated by BRENDA team
Alam, M.Z.; Mansor, M.F.; Jalal, K.C.
Optimization of lignin peroxidase production and stability by Phanerochaete chrysosporium using sewage-treatment-plant sludge as substrate in a stirred-tank bioreactor
J. Ind. Microbiol. Biotechnol.
36
757-764
2009
Phanerodontia chrysosporium
Manually annotated by BRENDA team
Wang, P.; Hu, X.; Cook, S.; Begonia, M.; Lee, K.; Hwang, H.
Effect of culture conditions on the production of ligninolytic enzymes by white rot fungi Phanerochaete chrysosporium (ATCC 20696) and separation of its lignin peroxidase
World J. Microbiol. Biotechnol.
24
2205-2212
2008
Phanerodontia chrysosporium, Phanerodontia chrysosporium ATCC 20696
-
Manually annotated by BRENDA team
Lee, K.; Pi, K.; Lee, K.
Synthesis of veratraldehyde from veratryl alcohol by lignin peroxidase with in situ electrogeneration of hydrogen peroxide in an electrochemical reactor
World J. Microbiol. Biotechnol.
25
1691-1694
2009
Phanerodontia chrysosporium, Phanerodontia chrysosporium ATCC 24725
Manually annotated by BRENDA team
Brueck, T.B.; Brueck, D.W.
Oxidative metabolism of the anti-cancer agent mitoxantrone by horseradish, lacto-and lignin peroxidase
Biochimie
93
217-226
2011
Phanerodontia chrysosporium
Manually annotated by BRENDA team
Wen, X.; Jia, Y.; Li, J.
Degradation of tetracycline and oxytetracycline by crude lignin peroxidase prepared from Phanerochaete chrysosporium--a white rot fungus
Chemosphere
75
1003-1007
2009
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F-1767
Manually annotated by BRENDA team
Tuisel, H.; Sinclair, R.; Bumpus, J.A.; Ashbaugh, W.; Brock, B.J.; Aust, S.D.
Lignin peroxidase H2 from Phanerochaete chrysosporium purification, characterization and stability to temperature and pH
Arch. Biochem. Biophys.
279
158-166
1990
Phanerodontia chrysosporium (P11542), Phanerodontia chrysosporium
Manually annotated by BRENDA team
Min, K.; Yum, T.; Kim, J.; Woo, H.M.; Kim, Y.; Sang, B.I.; Yoo, Y.J.; Kim, Y.H.; Um, Y.
Perspectives for biocatalytic lignin utilization cleaving 4-O-5 and Calpha-Cbeta bonds in dimeric lignin model compounds catalyzed by a promiscuous activity of tyrosinase
Biotechnol. Biofuels
10
212
2017
Agaricus bisporus, Phanerodontia chrysosporium
Manually annotated by BRENDA team
Vandana, T.; Kumar, S.; Swaraj, S.; Manpal, S.
Purification, characterization, and biodelignification potential of lignin peroxidase from immobilized Phanerochaete chrysosporium
BioResources
14
5380-5399
2019
Phanerodontia chrysosporium
-
Manually annotated by BRENDA team
Pham, L.T.M.; Seo, H.; Kim, K.J.; Kim, Y.H.
In silico-designed lignin peroxidase from Phanerochaete chrysosporium shows enhanced acid stability for depolymerization of lignin
Biotechnol. Biofuels
11
325
2018
Phanerodontia chrysosporium (P06181), Phanerodontia chrysosporium
Manually annotated by BRENDA team
Pham, L.T.M.; Deng, K.; Northen, T.R.; Singer, S.W.; Adams, P.D.; Simmons, B.A.; Sale, K.L.
Experimental and theoretical insights into the effects of pH on catalysis of bond-cleavage by the lignin peroxidase isozyme H8 from Phanerochaete chrysosporium
Biotechnol. Biofuels
14
108
2021
Phanerodontia chrysosporium (P06181), Phanerodontia chrysosporium
Manually annotated by BRENDA team
Khatoon, N.; Jamal, A.; Ali, M.I.
Lignin peroxidase isoenzyme a novel approach to biodegrade the toxic synthetic polymer waste
Environ. Technol.
40
1366-1375
2019
Phanerodontia chrysosporium, Phanerodontia chrysosporium NK-1
Manually annotated by BRENDA team
Biko, O.; Viljoen-Bloom, M.; van Zyl, W.
Microbial lignin peroxidases applications, production challenges and future perspectives
Enzyme Microb. Technol.
141
109669
2020
Phanerodontia chrysosporium (D1M7B6)
Manually annotated by BRENDA team
Son, H.; Seo, H.; Han, S.; Kim, S.M.; Pham, L.T.M.; Khan, M.F.; Sung, H.J.; Kang, S.H.; Kim, K.J.; Kim, Y.H.
Extra disulfide and ionic salt bridge improves the thermostability of lignin peroxidase H8 under acidic condition
Enzyme Microb. Technol.
148
109803
2021
Phanerodontia chrysosporium (P06181)
Manually annotated by BRENDA team
Houtman, C.J.; Maligaspe, E.; Hunt, C.G.; Fernandez-Fueyo, E.; Martinez, A.T.; Hammel, K.E.
Fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant
J. Biol. Chem.
293
4702-4712
2018
Phanerodontia chrysosporium (P06181)
Manually annotated by BRENDA team
Sadaqat, B.; Khatoon, N.; Malik, A.Y.; Jamal, A.; Farooq, U.; Ali, M.I.; He, H.; Liu, F.J.; Guo, H.; Urynowicz, M.; Wang, Q.; Huang, Z.
Enzymatic decolorization of melanin by lignin peroxidase from Phanerochaete chrysosporium
Sci. Rep.
10
20240
2020
Phanerodontia chrysosporium, Phanerodontia chrysosporium NK-1
Manually annotated by BRENDA team
Ecker, J.; Fueloep, L.
Lignin peroxidase ligand access channel dysfunction in the presence of atrazine
Sci. Rep.
8
5989
2018
Phanerodontia chrysosporium
Manually annotated by BRENDA team