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Enzyme
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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)
The sequence of appearance of cell wall degrading enzymes of Rhizoctonia solani propagules was followed. Polygalacturonase (PG;
EC 3.2.1.15
) was induced earlier by sodium polypectate (NaPP) as compared with the induction of cellulase (Cx; EC 3.2.1.4) by carboxymethyl cellulose (CMC), cellobiose, or fibrous cellulose powder. Increasing CMC concentration to 0.5% shortened the time of Cx appearance. In Czapek medium containing citrus pectin, pectin lyase (PL; EC 4.2.2.10) was produced faster and at higher amounts than in a medium containing NaPP as the sole carbon source. PG appearance also preceded that of PL in media simultaneously supplemented with their respective inducers. NaPP, which induced production of PG, repressed Cx production. Among the Cx inducers, only CMC and cellobiose repressed PG production to any extent. At pH 6.0, either in a synthetic medium or on autoclaved bean hypocotyl segments, a delay in PG production as compared with Cx and Pl production was observed. Optimal pH levels for enzyme production and activity were 4.0 and 5.0 for PG, and 5.5 for Cx, and 8.0 and 7.5 for PL. PG was less repressed than Cx by glucose, cellobiose, and monogalacturonic acid, while PL was not affected.
Can J Microbiol 1975
Sep
PMID:Sequential production of polygalacturonase, cellulase, and pectin lyase by Rhizoctonia solani. 24 78
Correlation and regression analyses were carried out between the virulence (expressed as growth rate in apple fruits) and the secretion in vitro of three host wall-degrading enzymes by 119 isolates of Sclerotinia fructigena, most of which had been obtained following exposure of conidia to N-methyl-N'-nitro-N-nitroso-guanidine. Virulence was found to be significantly correlated (P less than 0-01) with alpha-L-arabinofuranosidase, but not with pectin esterase or, where enzyme interdependence had been statistically eliminated, with
polygalacturonase
. Approximately 35% of the total variability in virulence could be accounted for in terms of the three enzymes.
J Gen Microbiol 1975
Sep
PMID:Correlation of virulence with secretion in vitro of three wall-degrading enzymes in isolates of Sclerotinia fructigena obtained after mutagen treatment. 123 34
We have purified and isolated cDNAs encoding the beta subunit of tomato fruit
polygalacturonase
isoenzyme 1 (PG1), a cell wall protein that associates with, and apparently regulates, the catalytic PG2 polypeptides. Expression of the beta subunit is fruit specific and temporally separated from the expression of PG2 during fruit development. The 37- to 39-kD beta subunit is encoded as a 69-kD precursor protein containing a signal sequence and two propeptide domains. The mature protein is composed almost entirely of the novel 14-amino acid motif FTNYGxxGNGGxxx in which many of the phenylalanine residues are post-translationally modified. The unique structural features of the motif suggest an important role in the function of the protein and hence in the activity of PG1. The beta subunit may represent a class of bifunctional plant proteins that interact both with structural components of the cell wall and catalytic proteins to localize and/or regulate metabolic activities within the cell wall.
Plant Cell 1992
Sep
PMID:The beta subunit of tomato fruit polygalacturonase isoenzyme 1: isolation, characterization, and identification of unique structural features. 139 11
Phytomonas sp. isolated from Euphorbia characias was adapted to SDM-79 medium. Cells isolated in the early stationary phase of growth were analyzed for their capacity to utilize plant carbohydrates for their energy requirements. The cellulose-degrading enzymes amylase, amylomaltase, invertase, carboxymethylcellulase, and the pectin-degrading enzymes
polygalacturonase
and oligo-D-galactosiduronate lyase were present in Phytomonas sp. and were all, except for amylomaltase, excreted into the external medium. Glucose, fructose and mannose served as the major energy substrates. Catabolism of carbohydrates occurred mainly via aerobic glycolysis according to the Embden-Meyerhof pathway, of which all the enzymes were detected. Likewise, the end-products of glycolysis, acetate and pyruvate, glycerol, succinate and ethanol were detected in the culture medium, as were the enzymes responsible for their production. Mitochondria were incapable of oxidizing succinate, 2-oxoglutarate, pyruvate, malate and proline, but had a high capacity to oxidize glycerol 3-phosphate. This oxidation was completely inhibited by salicylhydroxamic acid. No cytochromes could be detected either in intact mitochondria or in sub-mitochondrial particles. Mitochondrial respiration was not inhibited by antimycin, azide or cyanide. The glycolytic enzymes, from hexokinase to phosphoglycerate kinase, and the enzymes glycerol kinase, glycerol-3-phosphate dehydrogenase, phosphoenolpyruvate carboxykinase, malate dehydrogenase and adenylate kinase, were all associated with glycosomes that had a buoyant density of about 1.24 g cm-1 in sucrose. Cytochemical staining revealed the presence of catalase in these organelles. The cytosolic enzyme pyruvate kinase was activated by fructose 2,6-bisphosphate, typical of all other pyruvate kinases from Kinetoplastida. The energy metabolism of the plant parasite Phytomonas sp. isolated from E. characias resembled that of the bloodstream form of the mammalian parasite Trypanosoma brucei.
Mol Biochem Parasitol 1992
Sep
PMID:Characterization of carbohydrate metabolism and demonstration of glycosomes in a Phytomonas sp. isolated from Euphorbia characias. 143 59
A water extraction of crushed leaves of Nerium oleander yielded 2.3% of a crude polysaccharide. The main fraction (67%) represents a pectic polysaccharide mainly composed of galacturonic acid besides rhamnose, arabinose and galactose. The polysaccharide structure was characterized by NMR, mild acid- and
pectinase
treatment combined with GC-MS analyses. In vivo tests for a possible antitumor activity did not result in a significant action. Investigation of immunomodulating activity brought some indications for mitogenic activity and a weak macrophage-mediated cytotoxicity. Increase of phagocytosis could not be doubtlessly assigned to the polysaccharide due to the high amount of endotoxin in the homogenous fraction OLE 2.
Pharmazie 1991
Sep
PMID:[Polysaccharides from Nerium oleander: structure and biological activity]. 179 30
A 1319 bp long cDNA encoding for a
polygalacturonase
(
EC 3.2.1.15
) from Aspergillus niger RH5344 comprises a single open reading frame of 1089 bp which includes the mature protein of 362 amino acids and an NH2-terminal signal peptide of 27 amino acids. The directly determined peptides of the mature
polygalacturonase
confirmed the sequence information deduced from the cDNA.
Biochim Biophys Acta 1990
Sep
10
PMID:Cloning and DNA sequence analysis of a polygalacturonase cDNA from Aspergillus niger RH5344. 240 Jul 85
Polygalacturonic acid was used as a ligand in the affinity technique for pectinases purification from the filtrate of Aspergillus niger 71 culture. For this purpose four matrices were examined, namely, alkylamine controlled porous glass (CPG), alkylamine silica gel as well as keratin or polyamide coated silica gel. Good results of
pectinase
purification was obtained on silanized CPG or keratin coated silica gel supports.
Biochem Biophys Res Commun 1985
Sep
16
PMID:New matrices for the purification of pectinases by affinity chromatography. 241 47
Ripening is a complex developmental process involving changes in the biochemistry, physiology and gene expression of the fruit. It is an active process characterised by changes in all cellular compartments. cDNA cloning has been used as an approach to analyse changes in gene expression during fruit ripening. This has revealed that several genes are switched on specifically during fruit ripening, including one encoding
polygalacturonase
(PG), a major cell wall protein. These cDNA clones have been used to study the expression of the genes in normal and ripening mutant fruits, and under environmental stress conditions. The PG gene has been isolated and it has been demonstrated that 1450 bases 5' of the coding region are sufficient for the tissue- and development-specific expression of a bacterial marker gene in transgenic tomatoes. Antisense RNA techniques have been developed to generate novel mutant tomatoes in which the biochemical function of this enzyme and its involvement in fruit softening has been tested.
Plant Mol Biol 1989
Sep
PMID:Control and manipulation of gene expression during tomato fruit ripening. 249 57
Scale tissues taken from cones of pendent Douglas-fir Pseudotsuga menziesii (Mirb.) Franco were treated with
pectinase
to dissociate nuclei for Feulgen staining. Hydration of fixed tissues with water or a graded series of ethyl alcohol before
pectinase
treatment resulted in distention and faint staining of nuclei and inadequate disintegration of cell walls. These problems were overcome by adopting citrate buffer hydration. Analysis of digitized scans of nuclei provided information about the distribution of the stained material in density classes and nuclear size which is usually unavailable through the conventional double wavelength DNA measuring method.
Stain Technol 1982
Sep
PMID:Use of pectinase to dissociate plant nuclei for squash preparations: effect of hydration procedures. 675 7
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.
Can J Microbiol 1980
Sep
PMID:Lytic enzymes in the autolysis of Schizophyllum commune with special reference to 1,3-alpha-glucanase. 697 66
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