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Information on EC 1.11.1.14 - lignin peroxidase
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1.11.1.14 lignin peroxidaseIUBMB 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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Word Map
- 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
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
+
=
+
+
+
+
=
+
+
+
Synonyms
lignin peroxidase, mushroom tyrosinase, ligninase, liph8, heme-containing peroxidase, lignin peroxidase isozyme h8, diarylpropane oxygenase, ligninase h8, alip-p3, lignin peroxidase h8, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
diarylpropane oxygenase
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-
-
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diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving)
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-
-
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ligninase I
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-
-
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oxygenase, diarylpropane
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
-
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oxidation
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-
-
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reduction
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-
-
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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.
CAS REGISTRY NUMBER
COMMENTARY
93792-13-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2
vanillin + hydroxyacetaldehyde + guaiacol
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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
-
?
1-phenyl-1,2-ethandiol + H2O2
? + 2 H2O
substrate of N246A mutant enzyme
-
-
?
1-phenyl-1-propanol + H2O2
? + 2 H2O
substrate of N246A mutant enzyme
-
-
?
1-phenyl-2-propanol + H2O2
? + 2 H2O
substrate of N246A mutant enzyme
-
-
?
1-phenylethanol + H2O2
? + 2 H2O
substrate of N246A mutant enzyme
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
activity of EC 1.11.1.13
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
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-
-
?
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
? + H2O
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-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
?
Azure B + 2 H+ + H2O2
oxidized Azure B + 2 H2O
dye decolorization, substrate of N246A mutant enzyme
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-
?
guaiacylglycerol-beta-guaiacyl ether + H2O2
glycerol + guaiacol + 2 H2O
GGE, substrate of mutant enzyme N246A
-
-
?
lignocellulose + H2O2
? + H2O
substrate is wheat straw lignocellulose
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-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
dye decolorization, substrate of N246A mutant enzyme
-
-
?
remazol brilliant blue R + H2O2
oxidized remazol brilliant blue R + 2 H2O
substrate of N246A mutant enzyme
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-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzoic acid + 2 H2O
substrate of N246A mutant enzyme
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-
?
additional information
?
-
enzyme DypB has a significant role in lignin degradation in Rhodococcus jostii RHA1, is able to oxidize both polymeric lignin and a lignin model compound, and appears to have both Mn(II) and lignin oxidation sites
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-
?
additional information
?
-
-
enzyme DypB has a significant role in lignin degradation in Rhodococcus jostii RHA1, is able to oxidize both polymeric lignin and a lignin model compound, and appears to have both Mn(II) and lignin oxidation sites
-
-
?
additional information
?
-
enzyme DypB degrades solvent-obtained fractions of a Kraft lignin. The recombinant mutant enzyme Rh_DypB shows a classical peroxidase activity which is significantly increased by adding Mn2+ ions, kinetic parameters for H2O2, Mn2+, ABTS, and 2,6-DMP are determined. The enzyme shows broad dye-decolorization activity, especially in the presence of Mn2+, oxidizes various aromatic monomers from lignin, and cleaves the guaiacylglycerol-beta-guaiacyl ether (GGE), i.e., the Calpha-Cbeta bond of the dimeric lignin model molecule of beta-O-4 linkages. Under optimized conditions, 2 mM GGE is fully cleaved by recombinant Rh_DypB, generating guaiacol in only 10 min, at a rate of 12.5 micromol/min/mg enzyme. Screening of oxidation activity on monomeric lignin model compounds, overview
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-
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additional information
?
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enzyme DypB degrades solvent-obtained fractions of a Kraft lignin. The recombinant mutant enzyme Rh_DypB shows a classical peroxidase activity which is significantly increased by adding Mn2+ ions, kinetic parameters for H2O2, Mn2+, ABTS, and 2,6-DMP are determined. The enzyme shows broad dye-decolorization activity, especially in the presence of Mn2+, oxidizes various aromatic monomers from lignin, and cleaves the guaiacylglycerol-beta-guaiacyl ether (GGE), i.e., the Calpha-Cbeta bond of the dimeric lignin model molecule of beta-O-4 linkages. Under optimized conditions, 2 mM GGE is fully cleaved by recombinant Rh_DypB, generating guaiacol in only 10 min, at a rate of 12.5 micromol/min/mg enzyme. Screening of oxidation activity on monomeric lignin model compounds, overview
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
enzyme DypB has a significant role in lignin degradation in Rhodococcus jostii RHA1, is able to oxidize both polymeric lignin and a lignin model compound, and appears to have both Mn(II) and lignin oxidation sites
-
-
?
additional information
?
-
-
enzyme DypB has a significant role in lignin degradation in Rhodococcus jostii RHA1, is able to oxidize both polymeric lignin and a lignin model compound, and appears to have both Mn(II) and lignin oxidation sites
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
14.9
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
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
17.5
2,6-dimethoxyphenol
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+
3.1
Mn(II)
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
additional information
additional information
Michaelis-Menten kinetics by mutant enzyme N246A
-
additional information
additional information
-
Michaelis-Menten kinetics by mutant enzyme N246A
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12.6
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 1.5 mM H2O2
15.4
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
0.45
2,6-dimethoxyphenol
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 1.5 mM H2O2
0.5
2,6-dimethoxyphenol
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 0.3 mM H2O2
21.3
H2O2
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 50 mM 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
34
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+
19
Mn(II)
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 1.5 mM H2O2
21.4
Mn(II)
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 0.3 mM H2O2
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.85
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 1.5 mM H2O2
0.99
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
0.015
2,6-dimethoxyphenol
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 1.5 mM H2O2
0.29
2,6-dimethoxyphenol
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 0.3 mM H2O2
710
H2O2
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 50 mM 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
850
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+
1.7
Mn(II)
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 1.5 mM H2O2
6.9
Mn(II)
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 0.3 mM H2O2
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
wild-type Rhodococcus jostii RHA1 shows hydrogen peroxide-dependent activity, whereas the DypB knockout strain shows no observable activity in the presence or absence of hydrogen peroxide and a significant decrease in activity compared to that of the wild-type strain
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
determination of the secondary structure of the N246A variant with alpha-helix and beta-strand content of about 29% and about 19%, respectively
additional information
-
determination of the secondary structure of the N246A variant with alpha-helix and beta-strand content of about 29% and about 19%, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 37
the recombinant enzyme maintains a large part of the starting activity following incubation for 24 h in this temperature range
63 - 65
the recombinant enzyme shows a good thermostability with a melting temperature of 63-65°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged N246A mutant enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
design of a synthetic gene encoding the N246A variant of DypB from Rhodococcus jostii strain RHA1 (Rh_DypB) is designed by back translation of the protein sequence, recombinant overexpression of His-tagged N246A mutant enzyme in Escherichia coli strain BL21(DE3), the enzyme is fully produced as folded holoenzyme, thus without the need for a further reconstitution step
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
peroxidases are well-known biocatalysts produced by all organisms, especially microorganisms, and used in a number of biotechnological applications
additional information
-
peroxidases are well-known biocatalysts produced by all organisms, especially microorganisms, and used in a number of biotechnological applications
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ahmad, M.; Roberts, J.N.; Hardiman, E.M.; Singh, R.; Eltis, L.D.; Bugg, T.D.
Identification of DypB from Rhodococcus jostii RHA1 as a lignin peroxidase
Biochemistry
50
5096-5107
2011
Rhodococcus jostii (Q0SE24), Rhodococcus jostii
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