Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.10.3.2 (laccase)
 4,656 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The ascomycete, Botryosphaeria sp, produced two extracellular constitutive laccases (PPO-I and PPO-II) active toward the substrates: 2, 2(1)-azino-bis(3-ethyl-benzthiazoline-6-sulfonic acid) [ABTS], and 2,6-dimethoxyphenol (DMP), respectively. The production of both laccases increased when the fungal isolate was grown in the presence of veratryl alcohol, and resulted in optimal laccase production (100- and 25- fold, respectively) at 40 mM. The effect of aeration on growth and laccase production was studied in baffled flasks, and showed that aeration of the cultures increased the production of both enzymes 4-5 fold in the presence of veratryl alcohol. Both laccases were susceptible to inhibition by azide, acetate and chloride anions. Veratryl alcohol inhibited the laccase-catalyzed polymerization of DMP. Growing cultures of Botryosphaeria sp. produced an exopolysaccharide of the beta-glucan type whose synthesis was depressed when grown in the presence of veratryl alcohol.
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PMID:The effects of aeration and veratryl alcohol on the production of two laccases by the ascomycete Botryosphaeria sp. 1111 1

The biochemical anti-herbivore defense of trembling aspen (Populus tremuloides Michx.) was investigated in a molecular analysis of polyphenol oxidase (PPO; EC 1.10.3.2). A PPO cDNA was isolated from a trembling aspen wounded leaf cDNA library and its nucleotide sequence determined. Southern analysis indicated the presence of two PPO genes in the trembling aspen genome. Expression of PPO was found to be induced after herbivory by forest tent caterpillar, by wounding, and by methyl jasmonate treatment. Wound induction was systemic, and occurred in unwounded leaves on wounded plants. This pattern of expression is consistent with a role of this enzyme in insect defense. A search for potential PPO substrates in ethanolic aspen leaf extracts using electron spin resonance (ESR) found no pre-existing diphenolic compounds. However, following a brief delay and several additions of oxygen, an ESR signal specific for catechol was detected. The source of this catechol was most likely the aspen phenolic glycosides tremulacin or salicortin which decomposed during ESR experiments. This was subsequently confirmed in experiments using pure salicortin.
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PMID:Polyphenol oxidase and herbivore defense in trembling aspen (Populus tremuloides): cDNA cloning, expression, and potential substrates. 1147 16

Polyphenol oxidase (PPO; EC 1.10.3.2) is the enzyme thought to be responsible for browning in banana [Musa cavendishii (AAA group, Cavendish subgroup) cv. Williams] fruit. Banana flesh was high in PPO activity throughout growth and ripening. Peel showed high levels of activity early in development but activity declined until ripening started and then remained constant. PPO activity in fruit was not substantially induced after wounding or treatment with 5-methyl jasmonate. Banana flowers and unexpanded leaf roll had high PPO activities with lower activities observed in mature leaves, roots and stem. Four different PPO cDNA clones were amplified from banana fruit (BPO1, BPO11, BPO34 and BPO35). Full-length cDNA and genomic clones were isolated for the most abundant sequence (BPO1) and the genomic clone was found to contain an 85-bp intron. Introns have not been previously found in PPO genes. Northern analysis revealed the presence of BPO1 mRNA in banana flesh early in development but little BPO1 mRNA was detected at the same stage in banana peel. BPO11 transcript was only detected in very young flesh and there was no detectable expression of BPO34 or BPO35 in developing fruit samples. PPO transcripts were also low throughout ripening in both flesh and peel. BPO1 transcripts were readily detected in flowers, stem, roots and leaf roll samples but were not detected in mature leaves. BPO11 showed a similar pattern of expression to BPO1 in these tissues but transcript levels were much lower. BPO34 and BPO35 mRNAs were only detected at a low level in flowers and roots and BPO34 transcript was detected in mature leaves, the only clone to do so. The results suggest that browning of banana fruit during ripening results from release of pre-existing PPO enzyme, which is synthesised very early in fruit development.
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PMID:Molecular cloning and characterisation of banana fruit polyphenol oxidase. 1167 79

Polyphenol oxidases (PPOs; EC 1.10.3.2 or EC 1.14.18.1) catalyzing the oxygen-dependent oxidation of phenols to quinones are ubiquitous among angiosperms and assumed to be involved in plant defense against pests and pathogens. In order to investigate the role of PPO in plant disease resistance, we made transgenic tomato ( Lycopersicon esculentum Mill. cv. Money Maker) plants that overexpressed a potato ( Solanum tuberosum L.) PPO cDNA under control of the cauliflower mosaic virus 35S promoter. The transgenic plants expressed up to 30-fold increases in PPO transcripts and 5- to 10-fold increases in PPO activity and immunodetectable PPO. As expected, these PPO-overexpressing transgenic plants oxidized the endogenous phenolic substrate pool at a higher rate than control plants. Three independent transgenic lines were selected to assess their interaction with the bacterial pathogen Pseudomonas syringae pv. tomato. The PPO-overexpressing tomato plants exhibited a great increase in resistance to P. syringae. Compared with control plants, these transgenic lines showed less severity of disease symptoms, with over 15-fold fewer lesions, and strong inhibition of bacterial growth, with over 100-fold reduction of bacterial population in the infected leaves. These results demonstrate the importance of PPO-mediated phenolic oxidation in restricting plant disease development.
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PMID:Overexpression of polyphenol oxidase in transgenic tomato plants results in enhanced bacterial disease resistance. 1202 73

Marinomonas mediterranea is a melanogenic marine bacterium that expresses two different polyphenol oxidases. One of them is a multipotent laccase able to oxidize a wide range of substrates. The second enzyme is an SDS-activated tyrosinase. Using transposon mutagenesis, a mutant affected in the regulation of both polyphenol oxidase activities and melanogenesis has been isolated. The sequencing of the gene disrupted by the mini-Tn10 transposon in this mutant indicates that it encodes a hybrid sensor kinase. This sensor kinase shows three phosphorylated conserved domains: the transmitter domain containing a histidine site typical of sensor kinases, a receiver domain with an aspartate residue and an additional phosphotransferase domain with a second conserved histidine. This structural organization is characteristic of kinases participating in a phosphorelay system. Northern blot and lacZ operon fusions indicate that the multipotent laccase activity is regulated not only by PpoS but also by growth phase at the transcriptional level. These results suggest that PPO activities and melanin synthesis play a role in the adaptive response of M. mediterranea to stressful environmental conditions.
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PMID:Regulation of polyphenol oxidase activities and melanin synthesis in Marinomonas mediterranea: identification of ppoS, a gene encoding a sensor histidine kinase. 1217 39

Polyphenol oxidase (PPO; EC 1.10.3.2 or EC 1.14.18.1) takes part in the response of tomato plants (Lycopersicon esculentum Mill.) to wounding and herbivore attack, mediated by the octadecanoid wound-signaling pathway. Wounding and methyl jasmonate (MeJA) induce expression of ppo genes and markedly increase the level of the enzyme. We report that pretreatment with MeJA also markedly increased the ability of isolated tomato chloroplasts to import and process PPO precursors (pPPO). Pea (Pisum sativum L.) chloroplasts showed no such response. Wounding or ethylene alone was ineffective but ethylene was synergistic with MeJA. Treatment with MeJA conferred a strong binding of pPPO, or its processing intermediate, to thylakoids and subsequent translocation into the lumen and processing to the mature protein. The effect on PPO import and translocation was evident after 8-16 h exposure to MeJA. Membrane-bound pPPO was cross-linked to a proteinaceous component of the thylakoid translocation apparatus, apparently induced by MeJA. The import and processing of other nuclear-encoded thylakoid proteins were not affected by MeJA in tomato. A 90-kDa protein that co-fractionated with thylakoids was induced along with the increase in competence for PPO import, and was identified as the proteinase-inhibitor multicystatin. It is concluded that the 90-kDa protein observed is part of the MeJA-induced defense response of tomato, not a component of the thylakoid translocation apparatus.
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PMID:Import of polyphenol oxidase by chloroplasts is enhanced by methyl jasmonate. 1502 49

Polyphenol oxidases (PPOs; EC 1.14.18.1 or EC 1.10.3.2) catalyze the oxidation of phenolics to quinones, highly reactive intermediates whose secondary reactions are responsible for much of the oxidative browning that accompanies plant senescence, wounding, and responses to pathogens. To assess the impact of PPO expression on resistance to Pseudomonas syringae pv. tomato we introduced a chimeric antisense potato PPO cDNA into tomato (Lycopersicon esculentum L.). Oxidation of caffeic acid, the dominant o-diphenolic aglycone of tomato foliage, was decreased ca. 40-fold by antisense expression of PPO. All members of the PPO gene family were downregulated: neither immunoreactive PPO nor PPO-specific mRNA were detectable in the transgenic plants. In addition, the antisense PPO construct suppressed inducible increases in PPO activity. Downregulation of PPO in antisense plants did not affect growth, development, or reproduction of greenhouse-grown plants. However, antisense PPO expression dramatically increased susceptibility to P. syringae expressing the avirulence gene avrPto in both Pto and pto backgrounds. In a compatible (pto) interaction, plants constitutively expressing an antisense PPO construct exhibited a 55-fold increase in bacterial growth, three times larger lesion area, and ten times more lesions cm(-2) than nontransformed plants. In an incompatible (Pto) interaction, antisense PPO plants exhibited 100-fold increases in bacterial growth and ten times more lesions cm(-2) than nontransformed plants. Although it is not clear whether hypersusceptibility of antisense plants is due to low constitutive PPO levels or failure to induce PPO upon infection, these findings suggest a critical role for PPO-catalyzed phenolic oxidation in limiting disease development. As a preliminary effort to understand the role of induced PPO in limiting disease development, we also examined the response of PPO promoter::beta-glucuronidase constructs when plants are challenged with P. syringae in both Pto and pto backgrounds. While PPO B inducibility was the same in both compatible and incompatible interactions, PPO D, E and F were induced to higher levels and with different expression patterns in incompatible interactions.
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PMID:Antisense downregulation of polyphenol oxidase results in enhanced disease susceptibility. 1530 Apr 39

Polyphenol oxidase activity (PPO, EC 1.14.18.1, monophenol monooxygenase, and EC 1.10.3.2, o-diphenoloxidase) has been extensively studied in banana fruit for its role in enzymatic browning. Rapid discolouration of leaf, stem and root tissue after injury and strong pigmentation of tissue extracts indicate that PPO and phenolic compounds are ubiquitous in vegetative tissue of banana as well. They hamper biochemical and molecular studies in banana, as cumbersome adaptations of extraction protocols are required. On the other hand, PPO and phenolic compounds could be an important part of the plant's defence system against pests and diseases, including root parasitic nematodes. To facilitate future studies in this area, extraction and assay conditions for PPO from roots of banana (Musa acuminata AAA, Grande naine) were optimized. Highest enzyme activities were obtained in a 0.2 M phosphate buffer at pH 7.0 with 5% insoluble polyvinylpyrrolidone and 0.25% Triton X-100. The lowest K(m) values were obtained for dopamine and D-catechin. Monophenolase activity was shown with p-cresol. Banana root PPO was strongly inhibited by dithiothreitol and sodium metabisulfite. In root sections, oxidation of dopamine strongly co-localized with aerenchyma in the cortex. The experiments revealed indications for the involvement of root PPO and dopamine in resistance of banana against the parasitic nematode Radopholus similis.
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PMID:Extraction and partial characterization of polyphenol oxidase from banana (Musa acuminata Grande naine) roots. 1681 56

Polyphenol oxidase (PPO; EC 1.10.3.2 or EC 1.14.18.1), a thylakoid-lumen protein encoded by a nuclear gene, plays a role in the defense of plants against both herbivores and pathogens. Although previously reported to be a Tat (twin-arginine-dependent translocation) protein, the import of PPO by isolated chloroplasts was inhibited by azide, a diagnostic inhibitor of the Sec-dependent pathway. Import of PPO inhibited thylakoid translocation of a Tat protein and did not affect translocation of Sec-dependent proteins. In contrast, a pre-accumulated iPPO competed with Sec-dependent but not with Tat proteins. A previously reported second processing step in the stroma removes a twin-Arg that is part of a 'Sec-avoidance' motif in the thylakoid targeting domain of PPO. When the second processing site was mutated, the import of the resulting precursor showed Sec-dependent characteristics. The PPO transit peptide could drive thylakoid translocation of a Tat protein in the dark. Azide inhibited the secretion of a PPO intermediate that lacks a twin-Arg to the periplasm of Escherichia coli, but had no effect on the export of the intermediate containing the twin-Arg. PPO is synthesized in plants in response to wound and pathogen-related signals and it is possible that when the Tat pathway is unable to translocate adequate amounts of newly synthesized PPO, translocation is diverted to the Sec-dependent pathway by processing the intermediate at the second site and removing the twin-Arg.
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PMID:Polyphenol oxidase can cross thylakoids by both the Tat and the Sec-dependent pathways: a putative role for two stromal processing sites. 1833 5

Polyphenol oxidase (PPO; EC 1.10.3.2) was isolated from wheat bran by a procedure that included ammonium sulfate fractionation, batch adsorption by DEAE-cellulofine, CM-cellulofine column chromatography, DEAE-cellulofine column chromatography, preparative isoelectric focusing, adsorption on the membrane of a Vivapure Q Maxi H spin column, and heat treatment. These procedures led to 150-fold purification with 4.2% recovery. The PPO was homogeneous by SDS/PAGE. The relative molecular weight of the PPO was estimated to be 37,000 based on its mobility in SDS/PAGE. The isoelectric point of the PPO was 4.4. The K(m) values of the PPO for caffeic acid, chlorogenic acid, pyrocatechol, 4-methyl catechol and l-DOPA as substrates were 0.077, 0.198, 1.176, 1.667 and 4.545 mM. The PPO was strongly inhibited by tropolone. The K(i) value for tropolone is 2.2 x 10(-7) M. The sequence of the 15 N-terminal amino-acid residues was determined to be ATDVRLSIAHQTRFA, which was identical to those of serpin from Triticum aestivum and protein Z from Hordeum vulgare. The PPO strongly inhibited the activity of trypsin, which is an enzyme of serine proteases; 50% inhibition was observed with 1.5 x 10(-7) M PPO. The K(i) value for PPO is 2.3 x 10(-8) M. The wheat bran PPO should be a very important protein for protecting wheat against disease, virus, insect and herbivore damages by both the activities of PPO and protease inhibitor.
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PMID:Polyphenol oxidase from wheat bran is a serpin. 1850 24


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