EC Number   |
General Information |
Reference |
|---|
   1.11.1.14 | evolution |
evolution of MnPs (EC 1.11.1.13) into LiPs (EC 1.11.1.1.14) parallels the removal of Mn2+ binding sites and the creation of surface tryptophan residues, which accelerates interaction with the bulky structure and oxidation of high-redox-potential substrates, such as lignin. Note that this evolution might unexpectedly result in poor acid stability of the modern LiP. Various white-rot fungi, such as Phanerochaete chrysosporium, Trametes sp., Coriolopsis byrsina, Phellinus rimosus, and Lentinus sp. possess LiP isozymes which are not stable under extremely acidic conditions (e.g. pH values lower than pH 3.0). Even though LiPs and MnPs share a similar overall structure, as both belong to members of the peroxidase family, MnPs found in fungi, such as Ceriporiopsis subvermispora and Pleurotus ostreatus, exhibit relatively higher stability under acidic pH conditions. The considerable acid stability observed could be a result of several noncovalent interactions, such as salt bridges and hydrogen bonding networks |
764351 |
| 1.11.1.14 | evolution |
isozyme lignin peroxidase A, LPA, is the major isozyme of the LP H8 family |
765049 |
| 1.11.1.14 | more |
lignin peroxidase is unable to degrade atrazine, analysis of the connection between the structural and dynamical properties of the enzyme and its incapability to degrade atrazine, protein-ligand docking and molecular dynamics study, three-dimensional modeling of the lignin peroxidase-atrazine complex, overview. Atrazine has no access to heme edge due to the electric charges of the delocalized S-triazine ring. The detected phenomenon suggests that the small size of the ligands only is not a sufficient condition to access the active site. Their physicochemical properties also influence the structural behaviour of the channel. The lignin peroxidase can directly oxidize lignin in the partially degraded plant cell walls cannot be excluded. Lignin peroxidase has a so-called ligand access channel which allows direct interaction between the substrate and the heme. Residues His82, Ile85, Glu146, Phe148, Asp183, Val184 and Gln222 are located in this channel. The channel is sterically restricted and does not allow access to large bulky (lignin) substrates. The enzyme's natural substrate, veratrol, can easily approach heme through the ligand access channel. Based on the results of protein-ligand docking, atrazine can find an energetically favourable position in the environment of the ligand channel residues, although, the mathematical probability of the formation of these complexes is not significant (10%, 16% and 53% frequency values at three different temperatures) |
765818 |
| 1.11.1.14 | more |
lignin peroxidases have a narrower heme access cavity than classical peroxidases, such as HRP and the low-redox potential fungal Coprinus cinerea peroxidase (CiP), which limits the interaction of the heme residue with some substrates and the oxidation thereof |
764607 |
| 1.11.1.14 | physiological function |
extracellular enzymes of white-rot fungi play an important role in the deconstruction of lignin in lignocellulosic biomass. Lignin peroxidase plays a role in biodegradation of plant cell wall lignin. LiP may also play a major role in the bio-delignification of lignocellulose in crop residues. Lignin peroxidase is an extracellular hemeprotein that is H2O2-dependent, with an unusually high redox potential and low optimum pH. It is capable of oxidizing a variety of reducing substrates, including polymeric substrates |
764314 |
| 1.11.1.14 | physiological function |
in native producers, LiP is secreted with veratryl alcohol (VA, 3,4-dimethoxybenzyl alcohol), a natural phenolic substrate of LiP that acts as a small diffusible redox mediator for the conversion of inaccessible substrates |
764607 |
| 1.11.1.14 | physiological function |
lignin peroxidases catalyze a variety of reactions, resulting in cleavage of both beta-O-4' ether bonds and C-C bonds in lignin, both of which are essential for depolymerizing lignin into fragments amendable to biological or chemical upgrading to valuable products. The pH is a key driving force for selective and efficient lignin peroxidase isozyme H8 catalyzed depolymerization of the phenolic lignin dimer |
764353 |
| 1.11.1.14 | physiological function |
LiP shows lignin degrading and coal depolymerization activity |
-, 711271 |
| 1.11.1.14 | physiological function |
peroxidases are considered essential agents of lignin degradation by white-rot basidiomycetes. Low-molecularweight oxidants likely have a primary role in lignin breakdown because many of these fungi delignify wood before its porosity has sufficiently increased for enzymes to infiltrate. It has been proposed that lignin peroxidases fulfill this role by oxidizing the secreted fungal metabolite veratryl alcohol to its aryl cation radical, releasing it to act as a one-electron lignin oxidant within woody plant cell walls, but the fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant. Isozyme LPA releases insignificant quantities of VA cation radical, and a different mechanism produces small ligninolytic oxidants during white rot |
765049 |
| 1.11.1.14 | physiological function |
Phanerochaete chrysosporium strain NK-1 is able to use polyvinyl chloride (PVC) as the sole source of carbon and energy, and this degradation of the polymer is mainly facilitated by the production of peroxidases. Thus, the enzyme production is considered as the function of cellular growth. Extracellular lignin peroxidases from Phanerocheate chrysosporium play a significant role in the degradation of complex polymeric compounds like PVC |
-, 764590 |
