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
-
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
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pH Range
pH Range on EC 1.11.1.14 - lignin peroxidase
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2.8 - 5.4
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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
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activity range, purified enzyme from immobilized Phanerochaete chrysosporium, profile overview
3 - 11
3 - 9
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activity range, optimal activity at pH 5.0, almost inactive at pH 11.0
additional information
high activity of veratryl alcohol oxidation at pH 2.6-5.0. The pH is a key driving force for selective and efficient lignin peroxidase isozyme H8 catalyzed depolymerization of the phenolic lignin dimer. Low pH conditions drive reaction equilibrium toward the favorable formation of the active cationic radical intermediate
additional information
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high activity of veratryl alcohol oxidation at pH 2.6-5.0. The pH is a key driving force for selective and efficient lignin peroxidase isozyme H8 catalyzed depolymerization of the phenolic lignin dimer. Low pH conditions drive reaction equilibrium toward the favorable formation of the active cationic radical intermediate