Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.15 (pectinase)
 2,440 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Recent studies have resulted in the proposal of a new species, Aeromonas schubertii (mannitol, sucrose, and indole negative), formerly termed Enteric Group 501, on the basis of the study of seven strains isolated from the southeastern and southwestern United States and Puerto Rico. We have isolated two phenotypically similar A. schubertii strains from infected human wounds sustained in the Chesapeake Bay area. Their identification was confirmed by DNA-DNA hybridization to the Centers for Disease Control definition strain 2446-81 (ATCC 43700) for group 12. The strains were further examined for the presence of virulence-associated markers: hemolysin, hemagglutinins, cytotoxin production, agglutination in acriflavine, resistance to normal human serum, and autoagglutination phenotype. Both strains were positive for hemolysin by the plate assay, cytotoxin production at 1:10, and DNase and protease. They were resistant to human serum and negative for acriflavine agglutination, and only one of the strains was autoagglutination positive. Both strains were negative for cell-free hemolysin, hemagglutinins, pectinase, and chitinase. These isolations of A. schubertii further extend its previously described geographic distribution and reinforce its role as a primary causative agent of cellulitis with possible increased antimicrobial resistance.
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PMID:Characterization of Aeromonas schubertii strains recently isolated from traumatic wound infections. 276 70

The pseudo-oligosaccharides, validamycins, showed potent inhibitory activity against trehalase of Rhizoctonia solani while no significant inhibition was exhibited against cellulase, pectinase, chitinase, alpha-amylase, alpha- and beta-glucosidases. In particular, validoxylamine A strongly inhibited trehalase in a competitive manner with a Ki value of 1.9 X 10(-9) M. The uptake of the antibiotic into the cell and the amount of the intracellular trehalose were investigated by incubating the washed mycelia of R. solani with validamycins. It was found that validamycin A is transported into the cell and hydrolyzed therein by a beta-glucosidase yielding validoxylamine A with greater inhibitory activity. Also validamycin A containing beta-D-glucosyl residue is more favorably taken up into the cell than validamycin D containing alpha-D-glucosyl residue or their common aglycone, validoxylamine A. In addition, validamycin A suppressed the in vivo degradation of the intracellular trehalose at very low concentration of 0.1 microgram/ml.
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PMID:Effect of validamycins on glycohydrolases of Rhizoctonia solani. 358 21

In the autolytic phase of growth Schizophyllum commune lost 62% of its dry weight in 70 days of incubation. The variations in the activity of some lytic enzymes were studied in the culture fluid and mycelial extracts during growth and autolysis of this fungus. The enzymes 1,3-beta-glucanase (exoglucanase), 1,3(4)-beta-glucanase (endoglucanase), alpha-amylase, and invertase behaved in the same way in culture fluid and mycelial extract, but their activities were much higher in the culture fluid. The enzyme activities increased during autolysis, but then decreased at the end of this period except in the case of alpha-amylase which remained high. It was only possible to detect 1,6-beta-glucanase, cellulase, and polygalacturonase activities at certain times during the autolytic phase of growth. The enzyme chitinase was not detected and 1,3-alpha-glucanase (S-glucanase) occurred in the mycelial extract at a higher concentration than in the culture fluid. A decrease in the activity of this enzyme in the mycelial extract and an increase in the culture fluid occurred during autolysis. The enzyme 1,3-alpha-glucanase exhibited two optima pH, one at 6.0 and the other at 8.0. The Km value for the latter was 0.02 M at pH 5.5 in borate-citrate-phosphate buffer.
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PMID:Lytic enzymes in the autolysis of Schizophyllum commune with special reference to 1,3-alpha-glucanase. 697 66

A suspension culture of white lupin cells has been established, and proteins of the exocellular matrix analysed. Based on homologies of N-terminal amino-acid sequences, three stress- or defence-related proteins: acidic class III chitinase, polygalacturonase-inhibiting protein, and germin/oxalate oxidase, secreted by lupin cell culture, were identified.
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PMID:Secretion of stress-related proteins by suspension-cultured Lupinus albus cells. 970 21

Treatment of tobacco (Nicotiana tabacum) cell-suspension cultures with cryptogein, an elicitin protein from Phytophthora cryptogea, resulted in the release of a factor(s) that diffused through a 1000-D cutoff dialysis membrane and was capable of inducing sesquiterpene cyclase enzyme activity (a key phytoalexin biosynthetic enzyme in solanaceous plants) when added to fresh cell-suspension cultures. The diffusible factor(s) was released from cells over a 20-h period and induced a more rapid induction of cyclase enzyme activity than did direct treatment of the cultures with pure elicitin protein. The diffusible factor also induced a more rapid accumulation of transcripts encoding for sesquiterpene cyclase, acidic and basic chitinase, and hsr203 (a putative hypersensitive response gene) than did elicitin treatment. The diffusible factor(s) was resistant to protease, pectinase, Dnase, and RNase treatments, was not extractable into organic solvents, and was not immunoprecipitable when challenged with polyclonal antibodies prepared against elicitin protein. The diffusible factor(s) could not induce the release of more factor, suggesting that it was a terminal signal. These results are consistent with the notion that cells directly challenged or stimulated by pathogen-derived elicitors release diffusible secondary signal molecules that orchestrate the induction of complementary defense responses in neighboring cells.
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PMID:Characterization of a Diffusible Signal Capable of Inducing Defense Gene Expression in Tobacco. 1222 30

A protocol for isolating and regenerating protoplasts from Trichothecium roseum has been described. Protoplasts from T. roseum were isolated using (i) a lytic enzyme combination composed of Novozym 234, chitinase, cellulase, and pectinase at a 5-mg/mL concentration and (ii) 0.6 M KCl as an osmotic stabilizer. A maximum number of 28 x 10(4) protoplasts/mL were obtained at pH 5.5. Experiments on the regeneration and reversion of protoplasts revealed a maximum regeneration (60.8%) in complete medium (potato dextrose--yeast extract agar) amended with 0.6 M KCl. The regenerated protoplasts were similar to the original parent strain in morphology, pigmentation, growth, and sporulation.
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PMID:Release and regeneration of protoplasts from the fungus Trichothecium roseum. 1289 35

Response surface analysis was used to determine optimum conditions [2% (w/v) chitin, 57.5 degrees C, 38 min] for microwave irradiation of chitin to improve its enzymatic hydrolysis. V(max)/K(m) of cabbage chitinase toward untreated and microwave-irradiated chitin was found to be 21.1 and 31.7 nmol h(-1) mg(-2) mL, respectively. Similar improvement was observed in the case of pectinase in its unusual catalytic activity of chitin degradation. It was found that a greater extent of chitin hydrolysis by chitinase was possible after the substrate chitin was irradiated with microwaves.
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PMID:Accelerating enzymatic hydrolysis of chitin by microwave pretreatment. 1465 36

The Colorless non-ripening (Cnr) mutation in tomato (Solanum lycopersicum) results in mature fruits with colorless pericarp tissue showing an excessive loss of cell adhesion (A.J. Thompson, M. Tor, C.S. Barry, J. Vrebalov, C. Orfila, M.C. Jarvis, J.J. Giovannoni, D. Grierson, G.B. Seymour [1999] Plant Physiol 120: 383-390). This pleiotropic mutation is an important tool for investigating the biochemical and molecular basis of cell separation during ripening. This study reports on the changes in enzyme activity associated with cell wall disassembly in Cnr and the effect of the mutation on the program of ripening-related gene expression. Real-time PCR and biochemical analysis demonstrated that the expression and activity of a range of cell wall-degrading enzymes was altered in Cnr during both development and ripening. These enzymes included polygalacturonase, pectinesterase (PE), galactanase, and xyloglucan endotransglycosylase. In the case of PE, the protein product of the ripening-related isoform PE2 was not detected in the mutant. In contrast with wild type, Cnr fruits were rich in basic chitinase and peroxidase activity. A microarray and differential screen were used to profile the pattern of gene expression in wild-type and Cnr fruits. They revealed a picture of the gene expression in the mutant that was largely consistent with the real-time PCR and biochemical experiments. Additionally, these experiments demonstrated that the Cnr mutation had a profound effect on many aspects of ripening-related gene expression. This included a severe reduction in the expression of ripening-related genes in mature fruits and indications of premature expression of some of these genes in immature fruits. The program of gene expression in Cnr resembles to some degree that found in dehiscence or abscission zones. We speculate that there is a link between events controlling cell separation in tomato, a fleshy fruit, and those involved in the formation of dehiscence zones in dry fruits.
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PMID:Effect of the Colorless non-ripening mutation on cell wall biochemistry and gene expression during tomato fruit development and ripening. 1556 27

The diversity and antifungal activity of fluorescent pseudomonads isolated from rhizospheres of tea, gladiolus, carnation and black gram grown in acidic soils with similar texture and climatic conditions were studied. Biochemical characterisation including antibiotic resistance assay, RAPD and PCR-RFLP studies revealed a largely homogenous population. At soil pH (5.2), the isolates exhibited growth with varying levels of siderophore production, irrespective of crop rhizospheres. Two isolates with maximum chitinase production showed antagonism. The bacterial populations in general lacked the ability to produce deleterious traits such as cellulase, pectinase and hydrogen cyanide. However, increased pH levels beyond 5.2 caused reduction in metabolite production with reduced antifungal activity. The homogeneity of the bacterial population irrespective of crop rhizospheres together with decreased secondary metabolite production at higher pH levels reinstated the importance of soil over host plant in influencing rhizosphere populations. The studies also yielded acid tolerant chitinase producing antagonistic fluorescent pseudomonads.
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PMID:Influence of soil reaction on diversity and antifungal activity of fluorescent pseudomonads in crop rhizospheres. 1684 55

Grapevine is subject to a number of diseases that affect yield and wine quality. To limit the excessive use of phytochemicals in the vineyard, alternative strategies have to be developed. Plant treatment with signaling molecules like elicitors stimulates their natural defense mechanisms. To improve grapevine tolerance against fungal pathogens, Vitis vinifera plants were treated with a natural exogenous elicitor, methyl jasmonate (MeJA). MeJA-treated leaves (Cabernet Sauvignon foliar cuttings) reacted by increasing transcript levels coding pathogenesis-related proteins (acidic class IV chitinase, serine protease inhibitor, polygalacturonase-inhibiting protein, and beta-1,3-glucanase) and coding enzymes involved in phytoalexin biosynthesis (one phenylalanine ammonia lyase and one stilbene synthase). This was correlated with the accumulation of stilbenes (antimicrobial compounds). The eliciting activity of MeJA was confirmed by enhanced tolerance of grapevine foliar cuttings and vineyard against powdery mildew (75% and 73%, respectively). On the basis of these original results, MeJA can therefore act as an efficient elicitor in an alternative strategy of grapevine protection.
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PMID:Methyl jasmonate induces defense responses in grapevine and triggers protection against Erysiphe necator. 1711 99


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