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
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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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Metals Ions
Metals Ions on EC 1.11.1.14 - lignin peroxidase
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Ca2+
Cu2+
Fe2+
Iron
Mn2+
Na+
additional information
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Mg2+ and Ca2+ fail to have any effect on the LiP activity
Ca2+
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each subunit of the homodimeric enzyme contains two Ca2+ ion binding sites
Iron
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hemoprotein containing protoporphyrin IX, high-spin ferri-heme-complex, 0.7 heme per enzyme molecule
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activity of manganese peroxidase progressively increases with concentration of Mn2+ to a maximum at about 1.8 mM, with a corresponding decrease in lignin peroxidase activity to less than 10%
Mn2+
1 mM, 5.4fold activation in assay with lignin. Presence of Mn2+ is required, Km value is 8.4 mM, and data are not consistent with DypB acting as a Mn peroxidase. Breakdown of wheat straw lignocellulose by recombinant enzyme is observed over 24-48 h in the presence of 1 mM MnCl2