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Information on EC 1.11.1.14 - lignin peroxidase

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EC Tree
     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.14 lignin peroxidase
IUBMB 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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UNIPROT: Q0SE24
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
mushroom tyrosinase, ligninase, heme-containing peroxidase, diarylpropane oxygenase, ligninase h8, alip-p3, lignin peroxidase liii, pr-lip1, pr-lip4, ligninase lg5, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diarylpropane oxygenase
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diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving)
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ligninase I
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oxygenase, diarylpropane
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
93792-13-3
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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-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2
vanillin + hydroxyacetaldehyde + guaiacol
show the reaction diagram
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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
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?
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
? + H2O
show the reaction diagram
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lignin + H2O2
? + H2O
show the reaction diagram
substrate is Kraft lignin
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?
lignocellulose + H2O2
? + H2O
show the reaction diagram
substrate is wheat straw lignocellulose
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?
additional information
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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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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Q0SE24
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.6
substrate 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
Q0SE24_RHOJR
Rhodococcus jostii (strain RHA1)
350
0
37222
TrEMBL
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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
Manually annotated by BRENDA team
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