This enzyme belongs to the family of
oxidoreductases, specifically those acting on a peroxide as acceptor (peroxidases) and can be included in the broad category of
ligninases. 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.
Background
Lignin is highly resistant to biodegradation and only higher fungi and some bacteria are capable of degrading the polymer via an oxidative process. This process has been studied extensively in the past twenty years, but the mechanism has not yet been fully elucidated.
Lignin is found to be degraded by enzyme lignin peroxidases produced by some fungi like Phanerochaete chrysosporium. The mechanism by which lignin peroxidase (LiP) interacts with the lignin polymer involves
veratrole alcohol, which is a secondary metabolite of white rot fungi that acts as a cofactor for the enzyme.
Structural studies
As of late 2007, 3
structures have been solved for this class of enzymes, with
PDB accession codes
1B80,
1B82, and
1B85.
References
K.E.L. Eriksson; R.A. Blanchette; P. Ander (1990). Microbial and Enzymatic Degradation of Wood and Wood Components. Springer-Verlag.
Cai DY, Tien M (1990). "Characterization of the oxycomplex of lignin peroxidases from Phanerochaete chrysosporium: equilibrium and kinetics studies". Biochemistry. 29 (8): 2085–91.
doi:
10.1021/bi00460a018.
PMID2328240.