Literature summary for 1.11.1.14 extracted from

Pham, L.T.M.; Seo, H.; Kim, K.J.; Kim, Y.H.
In silico-designed lignin peroxidase from Phanerochaete chrysosporium shows enhanced acid stability for depolymerization of lignin (2018), Biotechnol. Biofuels, 11, 325 .

Search for more literature for 1.11.1.14

Application

Application	Comment	Organism
degradation	LiPH8 showing high acid stability will be a crucial player in biomass valorization using selective depolymerization of lignin	Phanerodontia chrysosporium

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified enzyme, hanging drop vapor diffusion method, mixing of 0.001 ml of 8 mg/ml protein solution in 10 mM succinate buffer, pH 6.0, with 0.001 ml of reservoir solution containing 16% PEG 6000, and equilibration of the mixture against 0.5 ml of reservoir solution, 7 days at 20°C, X-ray diffraction structure determination and analysis at 1.67 A resolution, modeling	Phanerodontia chrysosporium

Protein Variants

Protein Variants	Comment	Organism
A55R/N156E/H239E	site-directed mutagenesis, a rationally designed variant, that demonstrates a 12.5fold increased half-life under extremely acidic conditions, 9.9fold increased catalytic efficiency toward veratryl alcohol, and a 7.8fold enhanced lignin model dimer conversion efficiency compared to those of native LiPH8. The mutant has two constructed salt bridges. See for structure: PDB ID 6A6Q. Introduction of strong ionic salt bridges based on computational design results in a LiPH8 variant with markedly improved stability, as well as higher activity under acidic pH conditions	Phanerodontia chrysosporium
additional information	design of active LiPH8 variants for increased stability in intensively acidic environments. Introduction of new strong salt bridges at effective locations and optimized interactions between charged residues and their environments are vital for active and stable LiP at acidic pH. Molecular dynamics (MD) simulation of the solvated structure under the desired conditions and calculating the Gibbs free energy of the variant are used for creating an acid-stable LiP variant, followed by protein X-ray crystallography	Phanerodontia chrysosporium

Organism

Organism	UniProt	Comment	Textmining
Phanerodontia chrysosporium	P06181	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	lignin peroxidase isozyme H8 from the white-rot fungus Phanerochaete chrysosporium (LiPH8) demonstrates a high redox potential and can efficiently catalyze the oxidation of veratryl alcohol, as well as the degradation of recalcitrant lignin	Phanerodontia chrysosporium	?	-	-

Synonyms

Synonyms	Comment	Organism
lignin peroxidase isozyme H8	-	Phanerodontia chrysosporium
LiPH8	-	Phanerodontia chrysosporium

Cofactor

Cofactor	Comment	Organism	Structure
heme	-	Phanerodontia chrysosporium

General Information

General Information	Comment	Organism
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	Phanerodontia chrysosporium

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Release 2023.1 (January 2023)