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PubMed1991

Cloning and characterization of a lignin peroxidase gene from the white-rot fungus Trametes versicolor.

Six putative lignin peroxidase (LIP) genes were isolated from a lambda EMBL3 phage library of the white-rot fungus, Trametes versicolor, using the Phanerochaete chrysosporium LIP cDNA CLG5 as the probe. Sequence analysis of one of the genes, VLG1, showed that its coding region is interrupted by six small introns (49-64 bp) and that it encodes a mature LIP protein (341 aa; Mr: 36,714) that is preceded by a 25 aa signal sequence. This protein has a relatively high degree of aa homology to the N-termini of the LIP proteins purified from T. versicolor and has an aa homology of 55-60% to the LIP proteins of P. chrysosporium, which is comparable to that found between P. chrysosporium and Phlebia radiata LIP proteins.

Amino Acid Sequence↗

PubMed1991

Mechanisms of redox interactions between lignin peroxidase and cellobiose:quinone oxidoreductase.

The mechanism of redox interactions between the heme-enzyme, lignin peroxidase (LiP), and the FAD-enzyme, cellobiose:quinone oxidoreductase (CBQ) (EC 1.1.5.1), was investigated under various conditions. Veratryl alcohol oxidation by LiP was inhibited by CBQ in the presence of cellobiose. Lineweaver-Burk plots at various CBQ concentrations suggest that this inhibition is non-competitive. The oxidation rate of the reduced CBQ (FADH2) by LiP plus H2O2 increased significantly only in the presence of veratryl alcohol. Furthermore, the cation radical derived from 1,2,4,5-tetramethoxybenzene was reduced by CBQ in the presence of cellobiose. It is concluded from these results that CBQ can reduce aromatic cation radicals and that veratryl alcohol acts as a radical mediator of the redox interactions between LiP and CBQ.

Carbohydrate Dehydrogenases↗

PubMed1993

Low pH crystal structure of glycosylated lignin peroxidase from Phanerochaete chrysosporium at 2.5 A resolution.

The heme-containing glycoprotein lignin peroxidase (pI 4.15) has been crystallized at pH 4.0. The structure of the peroxidase from the orthorhombic crystals has been determined by multiple isomorphous replacement. The model comprises all 343 amino acids, one heme molecule, and three sugar residues. It has been refined to an R-factor of 20.3%. The chain fold of residues 15 to 275 is in general similar to those of cytochrome c peroxidase. Despite binding of the heme to the same region and a similar arrangement of the proximal and distal histidine as in cytochrome c peroxidase a significantly larger distance of the iron ion to the proximal histidine is observed. Distinct electron density extending from Asn-257 and at the distal side of the heme indicates ordered sugar residues in the crystal.

Basidiomycota↗

PubMed1994

Participation of Mn(II) in the catalysis of laccase, manganese peroxidase and lignin peroxidase from Phelbia radiata.

Oxidation capacities of laccase, manganese peroxidase (MnP) and lignin peroxidase (LiP) from Phlebia radiata were compared using non-phenolic (veratryl alcohol and ABTS) and phenolic (syringaldazine, vanillalacetone and Phenol red) compounds as reducing substrates. The effect of Mn(II) on enzyme reactions was also studied. Highest specific activities were recorded with laccase in the oxidation of phenolic compounds or ABTS and irrespective of Mn(II) concentration. LiP and MnP oxidized all these substrates but only the catalysis of MnP was dependent upon Mn(II). Only LiP clearly oxidized veratryl alcohol. However, Mn(II) interfered with this reaction by repressing veratraldehyde formation. These results point to multiple participation of manganese ions, either as a reducing (Mn(II)) or oxidizing (Mn(III)) agent in the enzymatic reactions.

Benzothiazoles↗

PubMed1995

Lignan models as inhibitors of Phanerochaete chrysosporium lignin peroxidase.

The lignan 8,8'-bis-(methylenedioxy)cinnamic acid (BMDCA) is a powerful competitive inhibitor (K1 = 2.0 microM) of the lignin peroxidase (LiP) from Phanerochaete chrysosporium and of the extracellular peroxidase of Phlebia radiata (I0.5 = 10 microM). BMDCA derivatives with the same double bond system also inhibited these enzymes to some extent. If the double bonds were hydrogenated, the inhibitory effect was lost. HRP-VIII and HRP-XI were slightly inhibited by BMDCA (I0.5 > 50 microM) and two plant peroxidases described as efficient lignan synthesizers were unaffected. Liquid cultures of P chrysosporium did not discolour the dve Poly R478 when 250 microM of BMDCA was present.

Anthraquinones↗

PubMed1989

A lignin peroxidase-encoding cDNA from the white-rot fungus Phlebia radiata: characterization and expression in Trichoderma reesei.

The nucleotide sequence of a cDNA coding for a lignin peroxidase (Lgp) of the white-rot fungus, Phlebia radiata, has been determined. By amino acid (aa) sequencing, it has been shown that the protein product of this gene is the LIII Lgp of Pb. radiata. The isolated gene and the putative aa sequence are about 60% homologous to published Lgp sequences from the fungus, Phanerochaete chrysosporium. The aa thought to be involved in the catalysis of LIII are revealed by comparison with the yeast cytochrome c peroxidase. The P. radiata Lgp-encoding gene (lgp3) was expressed in the fungus, Trichoderma reesei, under the cellobiohydrolase-encoding cbh1 gene promoter. Lgp3 mRNA was produced by the T. reesei transformants. No Lgp protein, however, could be detected.

Agaricales↗

PubMed1991

Cloning of several lignin peroxidase (LIP)-encoding genes: sequence analysis of the LIP6 gene from the white-rot basidiomycete, Phanerochaete chrysosporium.

A Phanerochaete chrysosporium BKMF1767 genomic library, constructed in the BamHI site of vector YRp12, was screened with the lignin peroxidase(LIP)-encoding cDNAs, CLG4 and CLG5, that have been shown to encode LIP2 (previously H2) and LIP6 (previously H10), respectively. Six distinct LIP genomic clones, designated pGLG1, pGLG2, pGLG3, pGLG4, pGLG5, and pGLG6, were isolated in this study. Probe CLG4 hybridized only to pGLG1. Probe CLG5 gave intense hybridization to pGLG2 and weaker hybridization to clones pGLG3 through pGLG6, but showed little or no hybridization to pGLG1. These results, in agreement with previous biochemical results, indicate the existence of LIP gene subfamilies. The limits and transcriptional orientation of the LIP gene in each clone were determined. The sequence data showed that pGLG2 contains the LIP6 gene, which encodes a protein identical in amino acid (aa) composition to that encoded by CLG5. It contains a leader sequence of 27 aa and a mature protein of 344 aa (Mr 36,607). Archetypal TATA-box-like and CAAT-box-like sequences in the 5'-noncoding region are located 51 and 97 nt upstream from the cDNA start point, respectively. S1 nuclease analysis of the 5' region of LIP6 revealed two transcription start points 8 nt apart downstream from the TATA box. Comparison of the sequence of LIP6 with its corresponding cDNA CLG5 showed that the gene contains nine small introns which range in size from 50 to 62 bp. These introns contained consensus splice junction sequences similar to those reported in other fungal and yeast introns.

Amino Acid Sequence↗

PubMed1991

Lignin peroxidase from the basidiomycete Phanerochaete chrysosporium is synthesized as a preproenzyme.

The cDNA clone L18 encoding lignin peroxidase LiP2, the most highly expressed LiP isozyme from Phanerochaete chrysosporium strain OGC101, was isolated and sequenced. Comparison of the cDNA sequence with the N-terminal sequence of the mature LiP2 protein isolated from culture medium suggests that the mature protein contains 343 amino acids (aa) and is preceded by a 28-aa leader sequence. In vitro transcription followed by in vitro translation and processing by signal peptidase resulted in cleavage at a site following the Ala21 (counted from the N-terminal Met1 of the initial translation product). The resultant protein contains a 7-aa propeptide, indicating that LiP is synthesized as a preproenzyme.

Amino Acid Sequence↗

PubMed1996

A cluster of genes encoding major isozymes of lignin peroxidase and manganese peroxidase from the white-rot fungus Trametes versicolor.

A gene cluster from the white-rot basidiomycete Trametes (Coriolus) versicolor (Tv) PRL 572 containing three structural genes, LPGIII, LPGIV and MPGI, was characterized. The genes are arranged in the same transcriptional direction, within a 10-kb region, and found to encode quantitatively dominant isozymes of lignin peroxidase (LP) and manganese peroxidase (MP). The second gene in sequence, LPGIV, predicts a 346-amino-acid (aa) mature polypeptide (36.9 kDa, pI 4.31) which is identical with the partial aa sequence information available on the LP12 isozyme (43.1 kDa, pI 3.27). The first gene, LPGIII, encodes a 341-aa polypeptide (36.1 kDa, pI 3.93) which has not been identified at the protein level. However, the similarity of LPGIV would suggest that the predicted product is an LP-type enzyme. LPGIII and LPGIV are homologous to the tandemly arranged genes LPGII and LPGI, respectively, recently described by Jönsson and Nyman [Biochim. Biophys. Acta 1218 (1994) 408-412]. The homologous genes, LPGIII/LPGII and LPGIV/LPGI, are 99% and 96% identical in sequence, respectively, and are predicted to encode identical polypeptides, since base substitutions in the predicted exons are all synonymous. The third gene, MPGI, is different in intron-exon organization and predicted to be disrupted by five rather than six introns, as are the LP genes. The deduced polypeptide, 339 aa in size (35.9 kDa, pI 4.07), is identical with the partial aa sequence information available for isozyme MP2 (44.5 kDa, pI 3.09). The MPGI- and LPGIV-encoded polypeptides are 70% identical in sequence which suggests that MP and LP from Tv may be regarded as members of the same family within the plant peroxidase superfamily. Most importantly, this study identifies a gene encoding the MP2 isozyme, and further shows that genes encoding MP and LP can be closely linked on the chromosome and may be coordinately transcribed.

Base Sequence↗

PubMed1994

Do carbohydrates play a role in the lignin peroxidase cycle? Redox catalysis in the endergonic region of the driving force.

The redox cycle of lignin peroxidase (LiP) is discussed in terms of the Marcus theory of electron transfer. The difference in kinetic behaviour of the two redox couples LiP-Compound I/LiP-Compound II (LiPI/LiPII), respectively LiPII/LiP, in the oxidation of veratryl alcohol is attributed to an estimated increase in reorganization energy of about 0.5 eV for the conversion of LiPII to native enzyme compared to the reduction of LiPI to LiPII. Whereas LiPI/LiPII involves a transition from a low-spin oxyferryl prophyrin radical cation to a low-spin oxyferryl porphyrin system, the conversion of LiPII to native enzyme involves a change in spin-state to high-spin ferric, accompanied by a conformational change of the protein. In addition, a molecule of water is formed after protonation of the oxyferryl porphyrin system by the distal His-47 and Arg-43. Furthermore, the reduction of LiPI to LiPII is observed as an irreversible process. Since the oxidation of veratryl alcohol by oxidized LiP will occur in the endergonic region of the driving force, it is postulated that the thermodynamic unfavourable formation of veratryl alcohol radical cation is facilitated by reaction of a nucleophile with the incipient radical cation. It is further postulated that the ordered carbohydrate residues found near the entrance to the active site channel in the LiP crystal structure play a role in this process.

Aspartic Acid↗

PubMed2003

The roles of veratryl alcohol and nonionic surfactant in the oxidation of phenolic compounds by lignin peroxidase.

Veratryl alcohol (VA) at higher concentration stimulated the lignin peroxidase (LiP)-catalyzed oxidation of phenolic compounds remarkably. This novel phenomenon was due to its competition with the phenols for the active site of the enzyme and to the high reactivity of the formed cation radical of VA (VA+*) which resulted in an additional oxidation of the phenols. The influence of the nonionic surfactant Tween 80 on the VA-enhanced LiP-catalyzed oxidation of phenols depended on its concentration. At lower concentration it had a small synergetic effect but at higher concentration it decreased the initial rate. Studies of the capillary electrophoretic behavior of LiP in the presence of Tween 80 showed that this effect was caused by the surfactant aggregation on LiP which, at higher surfactant concentrations, might impede the access of VA to its binding site on LiP and, consequently, the VA+* formation.

Benzyl Alcohols↗

PubMed2005

Nano-assembly of manganese peroxidase and lignin peroxidase from P. chrysosporium for biocatalysis in aqueous and non-aqueous media.

Development, characterization, and activity studies of nano-assemblies of lignin peroxidase (LiP), and manganese peroxidase (MnP) from Phanerochaete chrysosporium on flat surfaces as well as colloidal particles have been investigated. These assemblies of LiP and MnP were fabricated with polyelectrolytes-poly(ethylenimine) (PEI), poly(dimethyldiallylammonium chloride) (PDDA), and poly(allylamine) (PAH)-using a layer-by-layer self-assembly technique (LbL). Characterization of these assemblies on flat surfaces was monitored using quartz crystal microbalance (QCM), while assemblies on microparticles such as melamine formaldehyde (MF) were carried out with zeta potential analyzer (ZPA). A unique dynamic adsorption-desorption of the enzyme layers is observed during the assembly. All the nano-assemblies of LiP and MnP can effectively oxidize veratryl alcohol (VA) to its aldehyde for an extended period of time. The effect of different polyions and the number of polyion layers on the activities of LiP and MnP nano-assembly was also examined. It is observed that drying of enzyme layer during the assembly and the use of non-aqueous media, such as acetone can significantly reduce the activity of the enzymes. Enzyme activity reaches a minimum when the concentration of acetone is increased to 30%; however, the activity can be restored to its original value by increasing the concentration of aqueous media. Preliminary studies using assemblies of LiP and MnP on MF microparticles further demonstrate the feasibility of developing potential systems for degradation of environmental pollutants.

Adsorption↗

PubMed2004

Lignin peroxidase is involved in the biobleaching of manganese-less oxygen-delignified hardwood kraft pulp by white-rot fungi in the solid-fermentation system.

Biobleaching of manganese-less oxygen-delignified hardwood kraft pulp (E-OKP) by the white-rot fungi Phanerochaete sordida YK-624 and P. chrysosporium was examined in the solid-state fermentation system. P. sordida YK-624 possessed a higher brightening activity than P. chrysosporium, increasing pulp brightness by 13.4 points after seven days of treatment. In these fermentation systems, lignin peroxidase (LiP) activity was detected as the principle ligninolytic enzyme, and manganese peroxidase and laccase activities were scarcely detected over the course of treatment of E-OKP by either fungus. Moreover, a linear relationship between brightness increase and cumulative LiP activity was observed under all tested culture conditions with P. sordida YK-624 and P. chrysosporium. These results indicated that LiP is involved in the brightening of E-OKP by both white-rot fungi.

Fermentation↗

PubMed2005

The two manganese peroxidases Pr-MnP2 and Pr-MnP3 of Phlebia radiata, a lignin-degrading basidiomycete, are phylogenetically and structurally divergent.

Two new, at primary sequence and protein structure levels different, manganese peroxidase encoding genes from the white rot basidiomycete Phlebia radiata are described. Both genes are expressed in liquid cultures of P. radiata containing milled alder wood or glucose as carbon source, and high Mn(2+) concentration. The gene Pr-mnp2 contains 7 introns and codes for a 390 amino-acid polypeptide, whereas Pr-mnp3 presents 11 introns and codes for a 362 amino-acid protein. The 3-D molecular models confirm this diversity; the predicted Pr-MnP2 with a long C-terminal extension has the highest structural similarity with the crystal structure of Phanerochaete chrysosporium MnP1, whereas the shorter Pr-MnP3 protein is structurally more related to lignin peroxidases (P. chrysosporium LiPH8/H2). In Pr-MnP3, however, an alanine replaces the exposed tryptophan present in LiP and versatile peroxidases, and both Pr-MnPs include the conserved Mn(2+)-binding amino-acid ligands. This is the first occasion when two enzymes of similar function and origin fall into phylogenetically distinct subfamilies within the expanding dendrogram of the class II fungal secretory heme peroxidases.

Amino Acid Sequence↗

PubMed2006

High efficient degradation of dyes with lignin peroxidase coupled with glucose oxidase.

The H(2)O(2) supply strategy was one of crucial factors for high efficient degradation of pollutants with lignin peroxidase (LiP). In this paper, an attempt was made to couple a H(2)O(2) producing enzymatic reaction to the LiP catalyzed oxidation of dyes. H(2)O(2) needed was generated by glucose oxidase (GOD) and its substrate glucose. The generation rate of H(2)O(2) could be easily controlled by adjusting the pH of the degradation system and the amount of GOD added. Due to the controlled release of H(2)O(2), a sustainable constant activity of LiP was observed. The inhibition of LiP by high level H(2)O(2) supplied externally by a single addition at the beginning of the experiments could be avoided. Degradation of three dyes (xylene cyanol, fuchsine and rhodamine B) with LiP coupled with GOD indicated that the present H(2)O(2) supply strategy was very effective for improvement of the efficiency of the decolourization of dyes.

Benzenesulfonates↗

PubMed2006

Changes in production of lignin degrading enzymes during interactions between mycelia of the tropical decomposer basidiomycetes Marasmiellus troyanus and Marasmius pallescens.

During the interaction of two tropical agaric fungi, Marasmius pallescens and Marasmiellus troyanus, on agar media, initial deadlock between the two mycelia was ultimately followed by take-over by M. troyanus. When shaken liquid cultures of these two fungi were mixed, a rapid increase in laccase and manganese peroxidase activity, but no lignin peroxidase, was detected in the culture supernatant. Even more rapid and elevated induction of laccase occurred when filter-sterilized supernatant of Marasmius pallescens was added to Marasmiellus troyanus cultures, but the reciprocal experiment (addition of M. troyanus supernatant to M. pallescens cultures), did not lead to any increase in laccase activity. Addition of autoclaved supernatant of M. pallescens also induced laccase activity from M. troyanus cultures, but over a period of days rather than hours. Although both M. troyanus, and to a lesser extent M. pallescens, are able to produce laccases in shaken liquid culture following addition of the inducer 2,5-dimethylalanine, these experiments suggest that the presence of heat-stable and heat-labile laccase inducers secreted by M. pallescens mycelia lead to induction of laccases by M. troyanus.

Aniline Compounds↗

PubMed2002

Spectrophotometric investigations with hexa-coordinate ferric lignin peroxidase: does water retention at the active site influence catalysis?

Native lignin peroxidase (LIP) can adopt either a stable penta- or hexa-coordinate state. We have examined catalysis with hexa-coordinate ferric LIP as the starting material, using rapid scanning spectrophotometry. Initial two-electron oxidation of hexa-coordinate native LIP by H(2)O(2) (Compound I formation) was accompanied by a shifting isosbestic point (419-->416 nm), consistent with displacement of a resident water molecule, prior to the reaction of the ferric iron with H(2)O(2). The Compound I species derived from a hexa-coordinate ferric state shows an unusual peak at 520 nm, which may be due to water retention in the vicinity of the heme active site. Compound I reduction by veratryl alcohol showed saturation kinetics, which contrasts with the situation observed when Compound I is derived from a penta-coordinate ferric state. The data inferred that water can interfere with heme access by electron donors, altering the mechanism of Compound I reduction.

Benzyl Alcohols↗

PubMed2003

One electron oxidation of benzyltrialkylsilanes catalysed by lignin peroxidase: comparison with the oxidation induced by chemical oxidants.

Lignin peroxidase catalyses the H(2)O(2)-induced oxidation of 4-methoxybenzyltrimethylsilane by an electron transfer mechanism. The intermediate radical cation undergoes preferentially C(alpha)[bond]H deprotonation to give 4-methoxybenzaldehyde whereas C(alpha)[bond]Si bond cleavage is a minor fragmentation pathway and leads to 4-methoxybenzyl alcohol. Similar results are obtained in the oxidation catalysed by the water soluble model compound 5,10,15,20-tetra(N-methyl-4-pyridyl)porphyrinatoiron(III) pentachloride. Instead, in the oxidation promoted by the genuine one-electron transfer oxidant potassium dodecatungstocobalt(III)ate C(alpha)[bond]Si bond cleavage is the exclusive fragmentation process of the intermediate radical cation. It is suggested that in the enzymatic and biomimetic oxidations of 4-methoxybenzyltrimethylsilane the deprotonation of the intermediate radical cation is promoted by the reduced form [PorFe(IV)[double bond]O] of the active oxidant, which is an iron-oxo porphyrin radical cation.

Electron Transport↗