KEGG   ENZYME: 1.11.1.14Help
Entry
EC 1.11.1.14                Enzyme                                 

Name
lignin peroxidase;
diarylpropane oxygenase;
ligninase I;
diarylpropane peroxidase;
LiP;
diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving);
1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol:hydrogen-peroxide oxidoreductase (incorrect);
(3,4-dimethoxyphenyl)methanol:hydrogen-peroxide oxidoreductase
Class
Oxidoreductases;
Acting on a peroxide as acceptor;
Peroxidases
BRITE hierarchy
Sysname
1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol:hydrogen-peroxide oxidoreductase
Reaction(IUBMB)
(1) 1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 3,4-dimethoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O [RN:R11501];
(2) 2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-dimethoxyphenyl)methanol radical + 2 H2O [RN:R11502]
Reaction(KEGG)
R11501 R11502;
(other) R04461
Show
Substrate
1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol [CPD:C21419];
H2O2 [CPD:C00027];
(3,4-dimethoxyphenyl)methanol [CPD:C21420]
Product
3,4-dimethoxybenzaldehyde [CPD:C02201];
2-methoxyphenol [CPD:C01502];
glycolaldehyde [CPD:C00266];
H2O [CPD:C00001];
(3,4-dimethoxyphenyl)methanol radical [CPD:C21421]
Comment
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.
History
EC 1.11.1.14 created 1992, modified 2006, modified 2011, modified 2016
Reference
1  [PMID:2982828]
  Authors
Kersten PJ, Tien M, Kalyanaraman B, Kirk TK.
  Title
The ligninase of Phanerochaete chrysosporium generates cation radicals from methoxybenzenes.
  Journal
J Biol Chem 260:2609-12 (1985)
Reference
2  [PMID:3080953]
  Authors
Paszczynski A, Huynh VB, Crawford R.
  Title
Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium.
  Journal
Arch Biochem Biophys 244:750-65 (1986)
DOI:10.1016/0003-9861(86)90644-2
Reference
3
  Authors
Harvey, P.J., Schoemaker, H.E. and Palmer, J.M.
  Title
Veratryl alcohol as a mediator and the role of radical cations in lignin biodegradation by Phanerochaete chrysosporium.
  Journal
FEBS Lett 195:242-246 (1986)
Reference
4  [PMID:2162833]
  Authors
Wariishi H, Marquez L, Dunford HB, Gold MH.
  Title
Lignin peroxidase compounds II and III. Spectral and kinetic characterization of reactions with peroxides.
  Journal
J Biol Chem 265:11137-42 (1990)
Reference
5  [PMID:2328240]
  Authors
Cai DY, Tien M.
  Title
Characterization of the oxycomplex of lignin peroxidases from Phanerochaete chrysosporium: equilibrium and kinetics studies.
  Journal
Biochemistry 29:2085-91 (1990)
Reference
6  [PMID:8527462]
  Authors
Khindaria A, Yamazaki I, Aust SD
  Title
Veratryl alcohol oxidation by lignin peroxidase.
  Journal
Biochemistry 34:16860-9 (1995)
Reference
7  [PMID:8639588]
  Authors
Khindaria A, Yamazaki I, Aust SD
  Title
Stabilization of the veratryl alcohol cation radical by lignin peroxidase.
  Journal
Biochemistry 35:6418-24 (1996)
DOI:10.1021/bi9601666
Reference
8  [PMID:9369491]
  Authors
Khindaria A, Nie G, Aust SD
  Title
Detection and characterization of the lignin peroxidase compound II-veratryl alcohol cation radical complex.
  Journal
Biochemistry 36:14181-5 (1997)
DOI:10.1021/bi9715730
Reference
9  [PMID:9790672]
  Authors
Doyle WA, Blodig W, Veitch NC, Piontek K, Smith AT.
  Title
Two substrate interaction sites in lignin peroxidase revealed by site-directed mutagenesis.
  Journal
Biochemistry 37:15097-105 (1998)
DOI:10.1021/bi981633h
Reference
10 [PMID:25649492]
  Authors
Pollegioni L, Tonin F, Rosini E
  Title
Lignin-degrading enzymes.
  Journal
FEBS J 282:1190-213 (2015)
DOI:10.1111/febs.13224
Other DBs
ExplorEnz - The Enzyme Database: 1.11.1.14
IUBMB Enzyme Nomenclature: 1.11.1.14
ExPASy - ENZYME nomenclature database: 1.11.1.14
UM-BBD (Biocatalysis/Biodegradation Database): 1.11.1.14
BRENDA, the Enzyme Database: 1.11.1.14
CAS: 93792-13-3

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