Lignin peroxidase

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In enzymology, a lignin peroxidase (EC 1.11.1.14) is an enzyme that catalyzes the chemical reaction

1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol + H₂O₂ $\rightleftharpoons$ 3,4-dimethoxybenzaldehyde + 1-(3,4-dimethoxyphenyl)ethane-1,2-diol + H₂O

Thus, the two substrates of this enzyme are 1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol and H₂O₂, whereas its 3 products are 3,4-dimethoxybenzaldehyde, 1-(3,4-dimethoxyphenyl)ethane-1,2-diol, and H₂O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on a peroxide as acceptor (peroxidases). The systematic name of this enzyme class is 1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol:hydrogen-peroxide oxidoreductase. Other names in common use include diarylpropane oxygenase, ligninase I, diarylpropane peroxidase, LiP, diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving). It employs one cofactor, heme.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1B80, 1B82, and 1B85.

[edit] References

IUBMB entry for 1.11.1.14
BRENDA references for 1.11.1.14 (Recommended.)
PubMed references for 1.11.1.14
PubMed Central references for 1.11.1.14
Google Scholar references for 1.11.1.14
Paszczynski A, Huynh VB, Crawford R (1986). "Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium". Arch. Biochem. Biophys. 244: 750–65. doi:10.1016/0003-9861(86)90644-2. PMID 3080953.
Renganathan V, Miki K, Gold MH (1985). "Multiple molecular forms of diarylpropane oxygenase, an H2O2-requiring, lignin-degrading enzyme from Phanerochaete chrysosporium". Arch. Biochem. Biophys. 241: 304–14. doi:10.1016/0003-9861(85)90387-X. PMID 4026322.
Tien M and Kirk TT (1984). "Lignin-degrading enzyme from Phanerochaete chrysosporium purification, characterization, and catalytic properties of a unique H2O2-requiring oxygenase". Proc. Natl. Acad. Sci. USA 81: 2280–2284. doi:10.1073/pnas.81.8.2280.
Doyle WA, Blodig W, Veitch NC, Piontek K, Smith AT (1998). "Two substrate interaction sites in lignin peroxidase revealed by site-directed mutagenesis". Biochemistry. 37: 15097–105. doi:10.1021/bi981633h. PMID 9790672.
Wariishi H, Marquez L, Dunford HB, Gold MH (1990). "Lignin peroxidase compounds II and III. Spectral and kinetic characterization of reactions with peroxides". J. Biol. Chem. 265: 11137–42. PMID 2162833.
Cai DY, Tien M (1990). "Characterization of the oxycomplex of lignin peroxidases from Phanerochaete chrysosporium: equilibrium and kinetics studies". Biochemistry. 29: 2085–91. doi:10.1021/bi00460a018. PMID 2328240.
Tien M, Tu CP (1987). "Cloning and sequencing of a cDNA for a ligninase from Phanerochaete chrysosporium". Nature. 326: 520–3. doi:10.1038/326520a0. PMID 3561490.
Renganathan V, Miki K, Gold MH (1986). "Role of molecular oxygen in lignin peroxidase reactions". Arch. Biochem. Biophys. 246: 155–61. doi:10.1016/0003-9861(86)90459-5. PMID 3754412.
Kersten PJ, Tien M, Kalyanaraman B, Kirk TK (1985). "The ligninase of Phanerochaete chrysosporium generates cation radicals from methoxybenzenes". J. Biol. Chem. 260: 2609–12. PMID 2982828.
Kirk TK, Farrell RL (1987). "Enzymatic "combustion": the microbial degradation of lignin". Annu. Rev. Microbiol. 41: 465–505. doi:10.1146/annurev.mi.41.100187.002341. PMID 3318677.