Investigation of the Substrate Specificity of Peroxidase Isoenzymes Occurring in Wood of Different Species

Stich, Karl; Ebermann, Robert

doi:10.1515/hfsg.1988.42.4.221

Cited by 15 publications

(8 citation statements)

References 13 publications

(12 reference statements)

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“…Nielsen et al, 2001;Quiroga et al, 2001), but kinetic data regarding pCA oxidation is scarce. Peroxidase activities for pCA that are higher or comparable to that for CA have been reported from both softand hardwood species (Stich and Ebermann, 1988;McDougall, 2001). …”

Section: Discussionmentioning

confidence: 75%

Characterization of basic p-coumaryl and coniferyl alcohol oxidizing peroxidases from a lignin-forming Picea abies suspension culture

et al. 2005

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A Norway spruce (Picea abies) tissue culture line that produces extracellular lignin into the culture medium has been used as a model system to study the enzymes involved in lignin polymerization. We report here the purification of two highly basic culture medium peroxidases, PAPX4 and PAPX5, and isolation of the corresponding cDNAs. Both isoforms had high affinity to monolignols with apparent K(m) values in microM range. PAPX4 favoured coniferyl alcohol with a six-fold higher catalytic efficiency (V(max)/K(m)) and PAPX5 p-coumaryl alcohol with a two-fold higher catalytic efficiency as compared to the other monolignol. Thus coniferyl and p-coumaryl alcohol could be preferentially oxidized by different peroxidase isoforms in this suspension culture, which may reflect a control mechanism for the incorporation of different monolignols into the cell wall. Dehydrogenation polymers produced by the isoforms were structurally similar. All differed from the released suspension culture lignin and milled wood lignin, in accordance with previous observations on the major effects that e.g. cell wall context, rate of monolignol feeding and other proteins have on polymerisation. Amino acid residues shown to be involved in monolignol binding in the lignification-related Arabidopsis ATPA2 peroxidase were nearly identical in PAPX4 and PAPX5. This similarity extended to other peroxidases involved in lignification, suggesting that a preferential structural organization of the substrate access channel for monolignol oxidation might exist in both angiosperms and gymnosperms.

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Section: Discussionmentioning

confidence: 75%

Characterization of basic p-coumaryl and coniferyl alcohol oxidizing peroxidases from a lignin-forming Picea abies suspension culture

et al. 2005

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“…Peroxidase activity was detected in the same parts of the tissue where accumulation of flavonoids also occurred. It may be therefore possible that the response to E. amylovora infections may be derived by the action of peroxidases and flavonoids in an intensified process of lignification postulated to contribute to plant-cell wall strengthening during plant-pathogen interaction (MÄDER & AMBERG-FISHER 1982;MÄDER & FÜSSL 1982;STICH & EBERMANN 1988). The differences in increase of lignification, peroxidase and flavonoid activity in plants in response to infections with E. amylovora strains of distinct virulence may be due to plant susceptibility and to differences in the degree to which the strain affect biochemical plant cell processes.…”

Section: Discussionmentioning

confidence: 99%

Spread of fire blight in Austria and Hungary - variability of Erwinia amylovora strains

Keck¹,

Hevesi²,

Ruppitsch³

et al. 2002

Plant Prot. Sci.

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First outbreaks of fire blight were detected in Austria in 1993 and in Hungary in 1995. 137 Erwinia amylovora isolates were compared by PCR-RFLP, sequencing of the repeat region of the PstI fragment of plasmid pEA29, RAPD and AFLP analysis. Differences of repeat numbers in first isolates were observed. Six isolates showed different RAPD profiles. In AFLP analysis, so far, no differences in fragment pattern were determined. Pathogenicity tests with micropropagated apple cultivars revealed differences in plant susceptibility and in virulence of isolates. Responses of Malus tissue were visualized by the use of epifluorescence microscopy through the localization and the production of substances involved in cellular defence mechanisms (e.g. flavonoids, lignin) in various susceptible cultivars. The effect of bacterial strains differing in pathogenicity is shown by cellular peroxidase and flavonoid production.

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“…Their studies indirectly suggest that the extracellular oxidative enzymes, or at least the substrate specificities of those enzymes responsible for monolignol polymerization, may change with respect to which monolignols are incorporated into lignin at particular stages of development. Work with peroxidases isolated from several tree species (29,33) suggests that differences in substrate specificity between particular isozymes could contribute to the developmental differences seen in lignin deposition. If laccase does contribute to lignin biosynthesis in vivo, its preference for sinapyl and coniferyl alcohols could likewise contribute to variations in lignin structure.…”

Section: Discussionmentioning

confidence: 99%

Laccase from Sycamore Maple (Acer pseudoplatanus) Polymerizes Monolignols

Sterjiades¹,

Dean²,

Eriksson³

1992

Plant Physiol.

267

189

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Current understanding of the final oxidative steps leading to lignin deposition in trees and other higher plants is limited with respect to what enzymes are involved, where they are localized, how they are transported, and what factors regulate them. With the use of cell suspension cultures of sycamore maple (Acer pseudoplatanus), an in-depth study of laccase, one of the oxidative enzymes possibly responsible for catalyzing the dehydrogenative polymerization of monolignols in the extracellular matrix, was undertaken. The time course for secretion of laccase into suspension culture medium was determined with respect to age and mass of the cells. Laccase was completely separated from peroxidase activity by hydrophobic interaction column chromatography, and its purity was assessed with different types of gel electrophoresis (isoelectric focusing-, native-, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis). Amino acid and glycosyl analyses of the purified enzyme were compared with those reported from previous studies of plant and fungal laccases. The specific activity of laccase toward several common substrates, including monolignols, was determined. Unlike a laccase purified from the Japanese lacquer tree (Rhus vernicifera), laccase from sycamore maple oxidized sinapyl, coniferyl, and p-coumaryl alcohols to form waterinsoluble polymers (dehydrogenation polymers). cambium extracts stimulated DHP formation from coniferyl alcohol more effectively than the addition of H202, from which he concluded that the combined actions of both laccase and peroxidase are important for lignin biosynthesis in plants (12). Subsequent studies of a purified laccase from the Japanese lacquer tree (Rhus vernicifera) found that the enzyme could not oxidize coniferyl alcohol to produce a DHP (26), thus supporting Higuchi's proposal and leading many researchers to believe that laccase plays no role in lignin biosynthesis. Further evidence to support the contention that laccase is not involved in lignin biosynthesis was provided by histochemical studies in which a chromogenic substrate for fungal laccases and peroxidases, syringaldazine, was oxidized when applied to lignifying plant tissues in the presence but not the absence of H202 (15).On the other hand, recent studies of plant laccase and peroxidase activities suggest that syringaldazine oxidation may not be an adequate marker for lignin-specific enzyme activity. In contrast to the results of Harkin and Obst (15), Goldberg et al. (14) found low levels of syringaldazine oxidation in poplar stem tissue sections even without the addition of H202; however, these authors attributed this to low levels of endogenous H202 in the tissues. Additionally, although syringaldazine has been found to be a good substrate for most, if not all, fungal laccases and peroxidases, it is not a substrate for at least one purified plant laccase (18), nor is it a substrate for an extracellular plant peroxidase whose synthesis is correlated with tissue lignification (9). Thus, Nakamura's demonstr...

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Investigation of the Substrate Specificity of Peroxidase Isoenzymes Occurring in Wood of Different Species

Cited by 15 publications

References 13 publications

Characterization of basic p-coumaryl and coniferyl alcohol oxidizing peroxidases from a lignin-forming Picea abies suspension culture

Characterization of basic p-coumaryl and coniferyl alcohol oxidizing peroxidases from a lignin-forming Picea abies suspension culture

Spread of fire blight in Austria and Hungary - variability of Erwinia amylovora strains

Laccase from Sycamore Maple (Acer pseudoplatanus) Polymerizes Monolignols

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