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Literature summary for 1.11.1.14 extracted from

  • Pham, L.T.M.; Deng, K.; Northen, T.R.; Singer, S.W.; Adams, P.D.; Simmons, B.A.; Sale, K.L.
    Experimental and theoretical insights into the effects of pH on catalysis of bond-cleavage by the lignin peroxidase isozyme H8 from Phanerochaete chrysosporium (2021), Biotechnol. Biofuels, 14, 108 .
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
A55R/N156E/H239E site-directed mutagenesis the triple mutant of LiPH8 with 2 additional saltbridges on the solvent-exposed regions shows excellent stability and oxidation activity under extremely acidic conditions down to pH 2.6. The stabilized mutant shows higher activity levels at all three pH levels tested, as compared to wild-type, with the highest activity at pH 2.6. Increased conversion of lignin dimer, convertion of 96.1% and 45.3% of the dimer at pH 2.6 and pH 5.0, respectively Phanerodontia chrysosporium
additional information engineering of lignin peroxidase isozyme H8 and other enzymes involved in lignin depolymerization including targeting stability at low pH. Catalysis of degradation of the dimer to products by an acid-stabilized variant of lignin peroxidase isozyme H8 increases from 38.4% at pH 5.0 to 92.5% at pH 2.6. At pH 2.6, the observed product distribution results from 65.5% beta-O-4' ether bond cleavage, 27.0% Calpha-C1 carbon bond cleavage, and 3.6% Calpha-oxidation as by-product Phanerodontia chrysosporium

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Phanerodontia chrysosporium selective and efficient lignin peroxidase isozyme H8 catalyzed depolymerization of the phenolic lignin dimer ?
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Organism

Organism UniProt Comment Textmining
Phanerodontia chrysosporium P06181
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Reaction

Reaction Comment Organism Reaction ID
2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-dimethoxyphenyl)methanol radical + 2 H2O proposed routes to bond-cleavage through a pre-protonation mechanism and an oxidation route and their respective protonated intermediates, reaction mechanism and pH-dependence, overview Phanerodontia chrysosporium
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 veratryl alcohol + H2O2
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 Phanerodontia chrysosporium 2 veratryl aldehyde + 2 H2O
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 ?
additional information selective and efficient lignin peroxidase isozyme H8 catalyzed depolymerization of the phenolic lignin dimer Phanerodontia chrysosporium ?
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additional information catalysis of degradation of the dimer to products by an acid-stabilized variant of lignin peroxidase isozyme H8 increases from 38.4% at pH 5.0 to 92.5% at pH 2.6. At pH 2.6, the observed product distribution results from 65.5% beta-O-4' ether bond cleavage, 27.0% Calpha-C1 carbon bond cleavage, and 3.6% Calpha-oxidation as by-product. Enzyme LiPH8 catalyzes the oxidative cleavage of both beta-O-4' ether and C-C bonds in aryl ether dimers and catalyzes breaking of beta-O-4' ether, C-C, and C-H bonds in trimeric lignin model compounds. The distribution of products is pH-dependent. Study catalysis of bond cleavage events in a phenolic lignin dimer by quantitative analysis of product formation during LiPH8-catalyzed degradation of a GGE model compound (GGE-NIMS compound) using nanostructure-initiator mass spectrometry. Low pH conditions drive reaction equilibrium toward the favorable formation of the active cationic radical intermediate. The cationic radical intermediate formed from LiPH8/H2O2-catalyzed 1-electron oxidation of GGE dimer is capable of undergoing a variety of reactions such as side-chain oxidation, C-C bond, and beta-O-4' ether bond cleavage. The intermediates are predicted from a heterolytic bond cleavage reaction mechanism when the first step 1-electron oxidation takes place at lower redox potential-Ring A. The deprotonation of the short-lived cationic radical results in the formation of the phenoxy radical which sequentially cleaved into fragments. Protonation of hydroxyl group under acidic conditions is a key step in bond-cleavage pathways Phanerodontia chrysosporium ?
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Synonyms

Synonyms Comment Organism
diarylpropane peroxidase UniProt Phanerodontia chrysosporium
lignin peroxidase isozyme H8
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 Phanerodontia chrysosporium
ligninase H8 UniProt Phanerodontia chrysosporium
LiPH8
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 Phanerodontia chrysosporium
LPOA
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 Phanerodontia chrysosporium

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3
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 the enzyme catalzes veratryl alcohol and non-phenolic lignin dimer oxidation with a pH optimum of 3.0 Phanerodontia chrysosporium

pH Range

pH Minimum pH Maximum Comment Organism
additional information
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 high activity of veratryl alcohol oxidation at pH 2.6-5.0. The pH is a key driving force for selective and efficient lignin peroxidase isozyme H8 catalyzed depolymerization of the phenolic lignin dimer. Low pH conditions drive reaction equilibrium toward the favorable formation of the active cationic radical intermediate Phanerodontia chrysosporium

General Information

General Information Comment Organism
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 Phanerodontia chrysosporium