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)

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

In vitro gene fusions were constructed between the polygalacturonase-encoding pehA gene of the Erwinia carotovora subsp. carotovora (Ecc) strain SCC3193 and the bla gene of pBR322. The gene fusions obtained (75-2, 75-5 and 75-6) encoded hybrid proteins with the entire signal peptide and 70, 260 or 327 amino acids (aa) of the mature 376 aa PehA protein, respectively, fused to the mature part of the periplasmic beta-lactamase. All three hybrid proteins remained cell-bound in Ecc. High-level expression of the longer fusions 75-5 and 75-6 in Ecc led to reduced growth and viability of the cells. This phenotype was utilized to select for spontaneous extragenic mutations restoring normal cell growth. Two classes of regulatory mutants were obtained by this selection. First, mutants impaired in the production of several exoenzymes, including polygalacturonase, were found. These were phenotypically similar to the previously characterized Exp- mutants. Secondly, mutants specifically impaired in the production of polygalacturonase (designated PehR-), but producing and secreting wild-type levels of pectate lyase and cellulase, were obtained. The PehR- mutations were shown to affect transcriptional activation of the pehA gene. Furthermore, the PehR- as well as PehA- mutants exhibited a reduced virulence phenotype suggesting that polygalacturonase is a virulence factor in Ecc.
Mol Gen Genet 1992 Jul
PMID:Expression of pehA-bla gene fusions in Erwinia carotovora subsp. carotovora and isolation of regulatory mutants affecting polygalacturonase production. 149 88

The production of pectinase was studied in Neurospora crassa, using the hyperproducer mutant exo-1, which synthesized and secreted five to six times more enzyme than the wild-type. Polygalacturonase, pectin lyase and pectate lyase were induced by pectin, and this induction was glucose-repressible. Polygalacturonase was induced by galactose four times more efficiently than by pectin; in contrast the activity of lyases was not affected by galactose. The inducing effect of galactose on polygalacturonase was not glucose-repressible. Extracellular pectinases were separated by ion exchange chromatography. Pectate and pectin lyases eluted into three main fractions containing both activities; polygalacturonase eluted as a single, symmetrical peak, apparently free of other protein contaminants, and was purified 56-fold. The purified polygalacturonase was a monomeric glycoprotein (38% carbohydrate content) of apparent molecular mass 36.6-37.0 kDa (Sephadex G-100 and urea-SDS-PAGE, respectively). The enzyme hydrolysed predominantly polypectate. Pectin was also hydrolysed, but at 7% of the rate for polypectate. Km and Vmax for polypectate hydrolysis were 5.0 mg ml-1 and 357 mumol min-1 (mg protein)-1, respectively. Temperature and pH optima were 45 degrees C and 6.0, respectively. The purified polygalacturonase reduced the viscosity of a sodium polypectate solution by 50% with an increase of 7% in reducing sugar groups. The products of hydrolysis at initial reaction times consisted of oligogalacturonates without detectable monomer. Thus, the purified Neurospora crassa enzyme was classified as an endopolygalacturonase [poly(1,4-alpha-D-galacturonide) glycanohydrolase; EC 3.2.1.15].
J Gen Microbiol 1991 Aug
PMID:Pectinase production by Neurospora crassa: purification and biochemical characterization of extracellular polygalacturonase activity. 183 96

Tomato plants were transformed with a chimaeric polygalacturonase (PG) gene, designed to produce a truncated PG transcript constitutively. In these plants expression of the endogenous PG gene was inhibited during ripening, resulting in a substantial reduction in PG mRNA and enzyme accumulation. This inhibition was comparable to that achieved previously using antisense genes. The expression of the truncated gene in ripe fruit was substantially lower than its expression in green fruit. Thus expression of both the endogenous and truncated genes is reduced in ripe fruit in which both are active. The implication of this observation is discussed in relation to the possible mechanism whereby sense constructs inhibit gene expression.
Mol Gen Genet 1990 Dec
PMID:Expression of a truncated tomato polygalacturonase gene inhibits expression of the endogenous gene in transgenic plants. 226 49

Polyacrylamide gel electrophoresis of extracellular pectinase and amylase isozymes of 170 mainly terverticillate Penicillium strains was undertaken. The data were coded and subjected to numerical analysis. Variation in intensity of isozymes was observed in repeat analyses of some strains, although most were consistent. Variation was also observed between some representative strains of species. P. viridicatum was more variable than P. brevicompactum and P. hordei for intensity of pectinase activity. There was a correlation between the grouping of the strains on the basis of the isozymes and the species concepts only in some cases. The method proved useful for the identification of strains producing intense activity which provided clear patterns, for example, P. brevicompactum and P. chrysogenum and to a lesser extent P. solitum var. crustosum and P. hordei. The method was also exclusionary in that some species were restricted to a particular cluster or subcluster. Amylase patterns confirmed that strains referred to as single species are not all homogeneous genetically, and that some strains are not simply haploid homokaryons. The genetic heterogeneity of the strains explains some of the problems in the systematics of the terverticillate penicillia.
J Gen Microbiol 1989 Nov
PMID:A reappraisal of the terverticillate penicillia using biochemical, physiological and morphological features. III. An evaluation of pectinase and amylase isoenzymes for species characterization. 248 30

Small bacteriocin is a low-molecular-weight bacteriocin which is common in fast-growing rhizobia. As its activity could not be detected in chloroform-sterilized culture supernatants (P.R. Hirsch, J. Gen. Microbiol. 113:219-228, 1979), the bacteriocin could not be purified in order to study its mechanism of action. We report here that small is soluble in chloroform, an observation which led to effective and simple (partial) purification. Other properties of small are its low molecular weight, which is estimated to be between 700 and 1,500, its resistance to proteolytic enzymes, pectinase, and lysozyme, and its heat stability at pH 5.5 but not at pH 7.0. Its bactericidal action on exponentially growing sensitive cells was not detected until 11 h after its addition. The bactericidal action was preceded by inhibition of cell division. To determine whether small activity is required for nodulation or nitrogen fixation, a transposon Tn5-induced small-negative mutant was isolated. The observation that this strain formed normal, acetylene-reducing root nodules showed that small production is not a prerequisite for the formation of effective nodules.
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PMID:Bacteriocin small of fast-growing rhizobia is chloroform soluble and is not required for effective nodulation. 399 74

The depolymerase activity of cell-free extracts of nine species of rumen ciliate protozoa and two mixed protozoal preparations, grown in vivo and in vitro, towards polygalacturonic acid was examined. The highest activity was found with Eremoplastron bovis and Ostracodinium obtusum bilobum while there was none in the spined or spineless forms of Entodinium caudatum and little in Polyplastron multivesticulatum. On the basis of the rapid drop in viscosity, inhibition by EDTA and the production of u.v.-absorbing material, the enzymes from all active species were designated as endopectate lyases (EC4.2.2.2) although some polygalacturonase may be present. Neither pectin nor polygalacturonic acid supported the survival or growth of any of the protozoal species tested.
J Gen Microbiol 1980 Oct
PMID:The degradation of polygalacturonic acid by rumen ciliate protozoa. 678 83

An extracellular pectinolytic enzyme produced by Butyrivibrio fibrisolvens isolated from the bovine rumen was studied. The enzyme had a pH optimum of 8.0 to 8.5 and was stimulated by Ca2+ and inhibited by EDTA. The products of pectinolysis had an absorption peak at 235 nm and reacted with thiobarbituric acid, indicating a lyase type of action. The enzyme cleaved the substrates terminally from the reducing end; action on poly- and oligogalacturonates resulted in the formation of an unsaturated trigalacturonate. The enzyme was classified as an exopectate lyase (EC 4.2.2.9). A pectinesterase was also produced by B. fibrisolvens but polygalacturonase was not detected.
J Gen Microbiol 1982 Nov
PMID:An exopectate lyase of Butyrivibrio fibrisolvens from the bovine rumen. 715 60

E.atroseptica 36A cells were transformed by the recombinant plasmids p27-1 and pEA364 (derivatives of the vector plasmid pUC19) containing pectate lyase genes of E.carotovora 17A and E.atroseptica 36A, respectively. The synthesis of pectate lyases determined by the cloned genes of bacteria of both subspecies, as well as the synthesis of the native enzymes, were induced by sodium poly pectate. Increase of the dose of pectate lyase genes did not result in alteration of pectate lyase secretion by E.atroseptica 36ApEA364 cells. At the same time, the efficiency of secretion of heterologous pectate lyases by E.atroseptica 36Ap27-1 cells was lower. The synthesis and secretion of the resident isoenzymes are as efficient as those of the parental cells. The results indicate a high specificity of the pectinase secretory system in Erwinia of different species and, moreover, subspecies.
Mol Gen Mikrobiol Virusol
PMID:[Expression of pectate lyase genes of Erwinia carotovora subsp. carotovora 17A and Erwinia carotovora subsp. atroseptica 36A in Erwinia carotovor substp. atroseptica 36A cells]. 773 92

Macrophage (M phi) chemiluminescence (CL) induced by interaction with the two types of colonial variants of Mycobacterium intracellulare was studied. A smooth, opaque and dome-shaped (SmD) colonial variant triggered more intense M phi CL than did a smooth, transparent and flat colonial variant (SmT). M phi CL-inducing activity of the SmD variant was reduced by heating or by treatments with either Pronase P, some endoglycosidases or Tween 80, thereby indicating that the SmD variant possesses M phi CL-inducing substance(s) having peptide, sugar and/or lipid-like moieties. Treatment of the SmD variant organism with some endoglycosidases, such as cellulase, pectinase, dextranase or alpha-amylase decreased its M phi CL-inducing ability. On the other hand, M phi CL-inducing activity of the SmT variant was not affected by any of above treatments except that it was slightly increased by Pronase P treatment and reduced by alpha-amylase and dextranase.
J Gen Microbiol 1993 Dec
PMID:Macrophage chemiluminescence induced by interaction with transparent and opaque colonial variants of Mycobacterium intracellulare. 812 27


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