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
-
1.11.1.14
-
chrysosporium
-
phanerochaete
-
manganese
-
laccase
-
melanin
-
ligninolytic
-
veratryl
-
peroxidases
-
melanoma
-
melanogenesis
-
white-rot
-
kojic
-
decolor
-
l-dopa
-
diphenolase
-
basidiomycete
-
trametes
-
monophenolase
-
versicolor
-
hyperpigmentation
-
lignin-degrading
-
whitening
-
textile
-
anti-tyrosinase
-
o-quinones
-
manganese-dependent
-
l-3,4-dihydroxyphenylalanine
-
microphthalmia-associated
-
anti-melanogenic
-
o-diphenols
-
bjerkandera
-
arbutin
-
skin-whitening
-
non-phenolic
-
1.14.18.1
-
dopaquinone
-
phlebia
-
tyrosinase-related
-
delignification
-
dopachrome
-
remazol
-
lignocellulolytic
-
anti-melanogenesis
-
eryngii
-
tyrosinases
-
catecholase
-
depigmenting
-
biotechnology
-
dye-decolorizing
-
synthesis
-
environmental protection
-
lignocellulose-degrading
-
analysis
-
degradation
-
industry
-
irpex
- 1.11.1.14
- chrysosporium
- phanerochaete
- manganese
- laccase
- melanin
-
ligninolytic
-
veratryl
- peroxidases
- melanoma
-
melanogenesis
-
white-rot
-
kojic
-
decolor
- l-dopa
- diphenolase
-
basidiomycete
- trametes
- monophenolase
- versicolor
- hyperpigmentation
-
lignin-degrading
-
whitening
-
textile
-
anti-tyrosinase
- o-quinones
-
manganese-dependent
- l-3,4-dihydroxyphenylalanine
-
microphthalmia-associated
-
anti-melanogenic
- o-diphenols
- bjerkandera
- arbutin
-
skin-whitening
-
non-phenolic
-
1.14.18.1
- dopaquinone
- phlebia
-
tyrosinase-related
-
delignification
- dopachrome
-
remazol
-
lignocellulolytic
-
anti-melanogenesis
- eryngii
- tyrosinases
- catecholase
-
depigmenting
- biotechnology
-
dye-decolorizing
- synthesis
- environmental protection
-
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
Advanced search results
KM Value
KM Value on EC 1.11.1.14 - lignin peroxidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
14.9
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 1.5 mM H2O2
15.6
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 0.3 mM H2O2
0.163
2,4-Dichlorophenol
-
mutant enzyme A140G/S190P/P193A/S196F/E208Q
0.19
2,4-Dichlorophenol
-
mutant enzyme P106R/S119R/N120T/S228Y/A272G/L275V/A315G/A317T
0.74
2,4-Dichlorophenol
-
mutant enzyme H102T/S119R/N120T/Q126K/A243R/A315G
0.755
2,4-Dichlorophenol
-
mutant enzyme P106R/Q210H/L211V/A243R/F255L
17.5
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 0.3 mM H2O2
29.5
2,6-dimethoxyphenol
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 1.5 mM H2O2
0.03
H2O2
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 50 mM 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
0.04
H2O2
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 50 mM 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and 2 mM Mn2+
0.083
H2O2
Loweporus lividus
-
2 mM veratryl alcohol, 50 mM sodium tartrate buffer pH 2.5, 25°C
4.09
H2O2
-
mutant enzyme P106R/S119R/N120T/S228Y/A272G/L275V/A315G/A317T
3.1
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 0.3 mM H2O2
11.2
Mn(II)
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 1.5 mM H2O2
0.054
veratryl alcohol
-
in 50 mM sodium tartrate buffer, at pH 2.5, 25°C
0.056
veratryl alcohol
-
pH 5.5, 30°C, purified enzyme from immobilized Phanerochaete chrysosporium
0.058
veratryl alcohol
Loweporus lividus
-
0.4 mM H2O2, 50 mM sodium tartrate buffer pH 2.5, 25°C
0.07
veratryl alcohol
-
pH 5.5, 30°C, purified enzyme from free Phanerochaete chrysosporium
0.588
veratryl alcohol
-
enzyme immobilized in xerogel matrix of trimethoxysilane and proplytetramethoxysilane, 25°C, pH 5.0
2.79
veratryl alcohol
recombinant enzyme without veratryl alcohol-H2O2 pretreatment, in 20 mM sodium succinate buffer (pH 3.0)
3.24
veratryl alcohol
recombinant enzyme with veratryl alcohol-H2O2 pretreatment, in 20 mM sodium succinate buffer (pH 3.0)
additional information
-
bioelectric oxidation of organic substrates by LiP immobilized on graphite electrode
-
additional information
additional information
-
Michalis-Menten kinetics
-
additional information
additional information
-
comparison of kinetic parameters of tyrosinase (EC 1.14.18.1) and lignin peroxidase (EC 1.11.1.14) (LiP) using veratryl alcohol as the substrate, overview
-
additional information
additional information
-
comparison of kinetic parameters of tyrosinase (EC 1.14.18.1) and lignin peroxidase (EC 1.11.1.14) (LiP) using veratryl alcohol as the substrate, overview
-
additional information
additional information
-
Michaelis-Menten analogous model is applied to fit experimental data of lignin oxidative degradation. The apparent Michaelis constant of purified LiP product (3.02 mg/ml) is lower than that of the crude LiP solution (4.74 mg/ml), and the apparent maximum reaction rate of the purified LiP product (1.15mg/ml/h) is higher than that of the crude LiP solution (0.86 mg/ml/h). The maximum Ytrs (49.8%) is obtained when the beta-glucosidase activity is 0. The activities of LiP, endo-beta-1,4-glucanase and exo-beta-1,4-glucanase are 10.77, 3.360 and 3.427 U/ml (3:1:1), respectively. The components and structure of the substrate is extremely different before and after synergistic action under optimal conditions. Comparison of kinetic parameters between crude enzyme solution and purified product, detailed overview
-
additional information
additional information
Michaelis-Menten kinetics by mutant enzyme N246A
-
additional information
additional information
-
Michaelis-Menten kinetics by mutant enzyme N246A
-
additional information
additional information
-
Michaelis-Menten kinetics. The Michaelis-Menten (MM) analogous model suitable for oxidation degradation reaction of lignin containing two parameters, including the apparent maximum rate (ma,max) and apparent Michael constant (ka,m), is deduced. The oxidation degradation of lignin in lignocellullosic biomass in a dilute solution system follows the MM analogous model
-