| Entry |
|
|---|
| Name |
lignin peroxidase;
diarylpropane oxygenase;
ligninase I;
diarylpropane peroxidase;
LiP;
diarylpropane:oxygen,hydrogen-peroxide oxidoreductase
(C-C-bond-cleaving) |
|---|
| Class |
Oxidoreductases;
Acting on a peroxide as acceptor;
Peroxidases
 |
|---|
| Sysname |
1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol:hydrogen-peroxide
oxidoreductase |
|---|
| Reaction(IUBMB) |
1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol + H2O2 =
3,4-dimethoxybenzaldehyde + 1-(3,4-dimethoxyphenyl)ethane-1,2-diol +
H2O [RN:R04461] |
|---|
| Reaction(KEGG) |
R04461
 |
|---|
| Substrate |
1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol [CPD:C04597];
H2O2 [CPD:C00027] |
|---|
| Product |
3,4-dimethoxybenzaldehyde [CPD:C02201];
1-(3,4-dimethoxyphenyl)ethane-1,2-diol [CPD:C16644];
H2O [CPD:C00001] |
|---|
| Cofactor |
Heme [CPD:C00032] |
|---|
| Comment |
A hemoprotein. Brings about the oxidative cleavage of C-C and ether
(C-O-C) bonds in a number of lignin model compounds (of the
diarylpropane and arylpropane-aryl ether type). The enzyme also
oxidizes benzyl alcohols to aldehydes, via an aromatic cation
radical [9]. Involved in the oxidative breakdown of lignin in white
rot basidiomycetes. Molecular oxygen may be involved in the reaction
of substrate radicals under aerobic conditions [3,8]. |
|---|
| Structures |
PDB: 1B80 1B82 1B85 |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:3080953]
Paszczynski A, Huynh VB, Crawford R.
Comparison of ligninase-I and peroxidase-M2 from the white-rot
fungus Phanerochaete chrysosporium.
Arch. Biochem. Biophys. 244 (1986) 750-65.
Phanerochaete chrysosporium |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:4026322]
Renganathan V, Miki K, Gold MH.
Multiple molecular forms of diarylpropane oxygenase, an
H2O2-requiring, lignin-degrading enzyme from Phanerochaete
chrysosporium.
Arch. Biochem. Biophys. 241 (1985) 304-14.
Phanerochaete chrysosporium |
|---|
Reference
Authors
Title
Journal
|
3
Tien, M. and Kirk, T.T.
Lignin-degrading enzyme from Phanerochaete chrysosporium;
purification, characterization, and catalytic properties of a unique
H2O2-requiring oxygenase.
Proc. Natl. Acad. Sci. USA 81 (1984) 2280-2284. |
|---|
Reference
Authors
Title
Journal
Organism
|
4 [PMID:9790672]
Doyle WA, Blodig W, Veitch NC, Piontek K, Smith AT.
Two substrate interaction sites in lignin peroxidase revealed by
site-directed mutagenesis.
Biochemistry. 37 (1998) 15097-105.
Phanerochaete chrysosporium |
|---|
Reference
Authors
Title
Journal
Organism
|
5 [PMID:2162833]
Wariishi H, Marquez L, Dunford HB, Gold MH.
Lignin peroxidase compounds II and III. Spectral and kinetic
characterization of reactions with peroxides.
J. Biol. Chem. 265 (1990) 11137-42.
Phanerochaete chrysosporium |
|---|
Reference
Authors
Title
Journal
Organism
|
6 [PMID:2328240]
Cai DY, Tien M.
Characterization of the oxycomplex of lignin peroxidases from
Phanerochaete chrysosporium: equilibrium and kinetics studies.
Biochemistry. 29 (1990) 2085-91.
Phanerochaete chrysosporium |
|---|
Reference
Authors
Title
Journal
Organism
|
7 [PMID:3561490]
Tien M, Tu CP.
Cloning and sequencing of a cDNA for a ligninase from Phanerochaete
chrysosporium.
Nature. 326 (1987) 520-3.
Phanerochaete chrysosporium |
|---|
Reference
Authors
Title
Journal
Organism
|
8 [PMID:3754412]
Renganathan V, Miki K, Gold MH.
Role of molecular oxygen in lignin peroxidase reactions.
Arch. Biochem. Biophys. 246 (1986) 155-61.
Phanerochaete chrysosporium |
|---|
Reference
Authors
Title
Journal
Organism
|
9 [PMID:2982828]
Kersten PJ, Tien M, Kalyanaraman B, Kirk TK.
The ligninase of Phanerochaete chrysosporium generates cation
radicals from methoxybenzenes.
J. Biol. Chem. 260 (1985) 2609-12.
Phanerochaete chrysosporium |
|---|
Reference
Authors
Title
Journal
|
10 [PMID:3318677]
Kirk TK, Farrell RL.
Enzymatic "combustion": the microbial degradation of
lignin.
Annu. Rev. Microbiol. 41 (1987) 465-505. |
|---|
| 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 |
|---|
