Information on EC 1.11.1.14 - lignin peroxidase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

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EC NUMBER
COMMENTARY hide
1.11.1.14
-
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RECOMMENDED NAME
GeneOntology No.
lignin peroxidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 3,4-dimethoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O
show the reaction diagram
(1)
-
-
-
2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-dimethoxyphenyl)methanol radical + 2 H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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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.
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CAS REGISTRY NUMBER
COMMENTARY hide
93792-13-3
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
NCIM 2890
-
-
Manually annotated by BRENDA team
strain MTCC 972
-
-
Manually annotated by BRENDA team
strain MTCC 972
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain BOS55
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
MTCC 2298
-
-
Manually annotated by BRENDA team
strain UVS
-
-
Manually annotated by BRENDA team
strain UVS
-
-
Manually annotated by BRENDA team
strain SXS 16
-
-
Manually annotated by BRENDA team
strain SXS 16
-
-
Manually annotated by BRENDA team
strain MTCC 1175
-
-
Manually annotated by BRENDA team
Inonotus linteus MTCC 1175
strain MTCC 1175
-
-
Manually annotated by BRENDA team
strain MTCC 141
-
-
Manually annotated by BRENDA team
MTCC-141
-
-
Manually annotated by BRENDA team
strain SXS48
-
-
Manually annotated by BRENDA team
strain SXS48
-
-
Manually annotated by BRENDA team
Lentinus strigellus
strain SXS 355
-
-
Manually annotated by BRENDA team
Lentinus strigellus SXS355
strain SXS 355
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Loweporus lividus
strain MTCC-1178
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain F. F. Lombard ME446 (ATCC 34 541)
-
-
Manually annotated by BRENDA team
ligninase LG5 precursor; strain H10
SwissProt
Manually annotated by BRENDA team
strain H2
SwissProt
Manually annotated by BRENDA team
ligninase H8 precursor; strain H8
SwissProt
Manually annotated by BRENDA team
strain MTCC 787
-
-
Manually annotated by BRENDA team
YK-624, ATCC 90872
UniProt
Manually annotated by BRENDA team
strain SXS 47
-
-
Manually annotated by BRENDA team
strain SXS 47
-
-
Manually annotated by BRENDA team
strain 79
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain MTCC 1803
-
-
Manually annotated by BRENDA team
strain MTCC 1807
-
-
Manually annotated by BRENDA team
strain MTCC 1807
-
-
Manually annotated by BRENDA team
Polyporous velutinus
strain MTCC 1813
-
-
Manually annotated by BRENDA team
Polyporous velutinus MTCC 1813
strain MTCC 1813
-
-
Manually annotated by BRENDA team
Pycnoporus sp.
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
strain MTCC 1812
-
-
Manually annotated by BRENDA team
strain MTCC 1812
-
-
Manually annotated by BRENDA team
strain MTCC 136
-
-
Manually annotated by BRENDA team
strain MTCC 136
-
-
Manually annotated by BRENDA team
strain SXS 43
-
-
Manually annotated by BRENDA team
strain MTCC 138
-
-
Manually annotated by BRENDA team
strain MTCC 957
-
-
Manually annotated by BRENDA team
strain MTCC 957
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-
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
1,4-dimethoxybenzene + H2O2
?
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
-
-
-
?
1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2
vanillin + hydroxyacetaldehyde + guaiacol
show the reaction diagram
-
Calpha-Cbeta bond cleavage of substrate takes place. This reaction is inhibited by addition of diaphorase, consistent with a radical mechanism for C-C bond cleavage
-
?
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
? + H2O
show the reaction diagram
-
-
-
?
2,4-dichlorophenol + H2O2
?
show the reaction diagram
2,6-dimethoxyphenol + H2O2
coerulignone + ?
show the reaction diagram
2-chloro-1,4-dimethoxybenzene
?
show the reaction diagram
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
show the reaction diagram
3-methyl-2-benzothiazolinone hydrazone + H2O2
? + H2O
show the reaction diagram
-
enzyme has several substrate binding sites for 3-methyl-2-benzothiazolinone hydrazone, in addition to low and high affinity binding sites for Mn2+
-
-
?
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-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
-
?
ferrocytochrome c + H2O2
?
show the reaction diagram
-
-
-
?
fuchsine + H2O2
?
show the reaction diagram
-
-
-
-
?
humic acid + H2O2
?
show the reaction diagram
humic acid + H2O2
? + H2O
show the reaction diagram
L-Dopa + H2O2
?
show the reaction diagram
lignin + H2O2
? + H2O
show the reaction diagram
lignocellulose + H2O2
? + H2O
show the reaction diagram
substrate is wheat straw lignocellulose
-
-
?
methylene blue + H2O2
? + H2O
show the reaction diagram
-
-
-
-
?
mimosine + H2O2
?
show the reaction diagram
mitoxantrone + H2O2
hexahydronaphtho-[2,3-f]-quinoxaline-7,12-dione + H2O
show the reaction diagram
-
low efficiency
-
-
?
n-propanol + H2O2
?
show the reaction diagram
-
-
-
-
?
n-propanol + H2O2
propanal + H2O
show the reaction diagram
n-propanol + H2O2
propanaldehyde + H2O
show the reaction diagram
n-propanol + H2O2
propionaldehyde + H2O
show the reaction diagram
-
-
-
-
?
non-phenolic substrates + H2O2
?
show the reaction diagram
oxytetracycline + H2O2
?
show the reaction diagram
pyrogallol red + H2O2
?
show the reaction diagram
-
-
-
-
?
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
-
-
?
reduced 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O
show the reaction diagram
-
-
-
?
rhodamine B + H2O2
?
show the reaction diagram
-
-
-
-
?
tetracycline + H2O2
?
show the reaction diagram
Trp + H2O2
?
show the reaction diagram
-
-
-
-
?
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
xylene cyanol + H2O2
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
veratryl alcohol + H2O2
?
show the reaction diagram
Q60FD2
-
-
-
?
additional information
?
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
1 mM, slight stimulation
Fe2+
-
1 mM, slight stimulation
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-bipyridyl
-
complete inhibition at 10 mM
Ag+
-
1 mM, about 80% inhibition of native enzyme, about 15% inhibition of enzyme immobilized in xerogel matrix of trimethoxysilane and proplytetramethoxysilane
Cetyltrimethylammonium bromide
-
weak
ethylenediamine
-
complete inhibition at 10 mM
L-cysteine
-
1 mM, complete inhibition of native enzyme, about 30% inhibition of enzyme immobilized in xerogel matrix of trimethoxysilane and proplytetramethoxysilane
Manganese
-
above 0.1 mM
NaCl
-
complete inhibition at 300 mM
sodium bis (2-ethylhexyl)-sulfosuccinate
-
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
tetramethylethylenediamine
-
complete inhibition at 8 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
H2O2
-
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
-
without veratryl alcohol in the reaction system, there are only 18% of tetracycline removal and 14% of oxytetracycline removal. The degradation percentage reaches its maximum with veratryl alcohol concentration larger than 2.0 mM for tetracycline and 1.5 mM for oxytetracycline
additional information
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.163 - 0.79
2,4-Dichlorophenol
0.106 - 0.318
2-chloro-1,4-dimethoxybenzene
6.2
Direct Blue GLL dye
-
-
0.03 - 23.6
H2O2
0.013
methylene blue
-
lignine peroxidas activity, pH 3.5, 25°C
1.57
Mn2+
-
mutant enzyme
0.5 - 1.6
n-Propanol
0.0271 - 3.24
veratryl alcohol
additional information
additional information
-
bioelectric oxidation of organic substrates by LiP immobilized on graphite electrode
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
37.1 - 333.3
2,4-Dichlorophenol
2.13 - 176.7
H2O2
0.18
methylene blue
-
lignin peroxidase activity, pH 3.5, 25°C
0.0467 - 17.7
veratryl alcohol
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
30
H2O2
-
pH 2.5, 25°C
35
veratryl alcohol
-
pH 2.5, 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4
NaN3
-
incompetitive
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.191
-
veratryl alcohol, yeast extract broth culture medium
0.307
-
n-propanol, yeast extract broth culture medium
2.2
-
isozyme TvLP2
3.68
Loweporus lividus
-
after DEAE-cellulose chromatogrphy
4.5
-
enzyme crude filtrate, pH 2.5, 25°C
8.4
-
veratryl alcohol
8.48
-
isozyme III
10.6
-
TvLP12
11.4
-
1,2-bis(3,4-di-methoxyphenyl)propane-1,3-diol
15.9
-
pH 3.0 tartrate buffer, 30°C
18.1
-
isozyme TvLP9
20.3
-
pH 3.0 tartrate buffer, 30°C
27.9
-
enzyme after 6.2fold purification, pH 2.5, 25°C
29.58
-
pH 2.5, 25°C
553
-
pH 6.0, 25°C
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 3.5
-
lignin peroxidase activity in absence of Mn2+
4.2
-
optimum pH for tetracycline and oxytetracycline degradation
4.5
-
1-(4'-ethoxy-3'-methoxy-phenyl)glycerol-beta-guaiacylether
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
-
enzyme immobilized in xerogel matrix of trimethoxysilane and proplytetramethoxysilane
6
-
native enzyme
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.8 - 3
Loweporus lividus
-
-
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 - 11
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26
Polyporous velutinus
-
-
60
-
native enzyme
80
-
enzyme immobilized in xerogel matrix of trimethoxysilane and proplytetramethoxysilane
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 90
15 - 30
Loweporus lividus
-
-
20 - 40
-
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
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
30 - 40
Pycnoporus sp.
-
highest LiP activity is detected at 37°C, followed by 30°C, and no activity is obeserved at 40°C
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17910
-
molecular ion [M-H]+, mass spectrometry
39000
-
x * 39000, isozyme I, SDS-PAGE
41000
-
x * 41000, isozyme II, SDS-PAGE
110000 - 130000
-
non-denaturing PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
isozyme H8 and W171 mutant
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
3
-
rapid inactivation
394601
3 - 6
-
native enzyme, stable for 1 h, enzyme immobilized in xerogel matrix of trimethoxysilane and proplytetramethoxysilane, stable for 24 h
724663
3 - 7
-
the recombiannt enzyme is stable from pH 3.5 to neutral pH, but unstable over pH 7.0 and below pH 3.0
701072
4.5 - 5.5
Lentinus strigellus
-
pH range preserving 70-100% of initial activity, 25°C, 24 h
702977
4.5 - 6
-
pH range preserving 70-100% of initial activity, 25°C, 24 h
702977
5 - 6
-
pH range preserving 70-100% of initial activity, 25°C, 24 h
702977
5.5 - 7
-
pH range preserving 70-100% of initial activity, 25°C, 24 h
702977
6 - 7
-
pH range preserving 70-100% of initial activity, 25°C, 24 h
702977
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 70
-
temperature range preserving 70-100% of initial activity, pH 5.0, 1 h
10 - 40
10 - 70
-
temperature range preserving 70-100% of initial activity, pH 5.0, 1 h
10 - 40
-
temperature range preserving 70-100% of initial activity, pH 5.0, 1 h
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
25
-
pH 7.0, 4 h, maximum activity loss of 10%
30 - 60
-
the recombinant enzyme is fully stable up to 30°C but unstable at 37°C, and is completely inactivated after 30 min at 60°C
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
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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.
-
tryptophan stabilizes the lignin peroxidase activity during decolorization of dyes
-
veratryl alcohol stabilizes at pH 3.5 and 23°C, lag-phases are not observed
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
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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
-
the concentrated enzyme can be stored without lost of activity for 2 months at 4°C in the refrigerator
Loweporus lividus
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
10 kDa ultrafiltration, 3 M ammonium sulphate precipitation, hydrophobic interaction chromatography, reversed phase chromatography
-
16 isozymes: TvLP1-16, differing in primary structure
-
3 isozymes by ion-exchange chromatography
-
at least 7 isozymes, LiP-1-7
-
DEAE-cellulose column chromatography
-
ion exchange chromatography, 4°C
-
Resource Q column chromatography, gel filtration
-
salt precipitation with 60% (NH4)2SO4, desalting column, Q FF ion exchange column and Sepharyl S-300 HR gel filtration
-
to homogeneity using Amicon concentration and DEAE cellulose chromatography
Loweporus lividus
-
ultrafiltration, anion-exchange and size exclusion chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)pLysS cells
-
expressed in Escherichia coli BL21(DE3)pLysS cells, recombinant LiP protein accumulates in inclusion bodies as an inactive form
-
expression in Escherichia coli
expression in Saccharomyces cerevisiae
-
homologous overexpression in Phanerochaete sordida YK-624 uracil auxotrophic mutant UV-64
overexpression of isozyme H8 and W171 mutant in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the C/N ratio of the optimized medium for LiP production composed of asparagines 9.967 g/l, urea 16.247 g/l, fructose 13.953 g/l, malt extract 12.58 g/l, and (NH4)2SO4 13.92 g/l is 1.433
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
N182D/D183K/A36E
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generating a Mn2+-binding site
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
W171F
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no activity towards veratryl alcohol
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the optimal refolding solution contains of 0.4 M urea, 5 mM CaCl2, 0.0005 mM hemin, and 0.6 mM oxidized glutathione in Tris-HCl buffer, at pH 9.5
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
biotechnology
degradation
environmental protection
synthesis
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LINKS TO OTHER DATABASES (specific for EC-Number 1.11.1.14)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)