Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.26 (invertase)
4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Pseudomonas syringae pv. phaseolicola, a plant pathogenic pseudomonad, possesses two sucrose-splitting enzymes, a levansucrase and a sucrase. The levansucrase is found both extracellularly and intracellularly, and enzyme synthesis is independent of the carbon source. In addition to levansucrase, cells grown on sucrose contain a sucrase. The two sucrose-splitting enzymes differ in their optimum pH value and optimum temperature as well as in their substrate specificities.
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PMID:[Detection and characterization of a levansucrase and a sucrase in Pseudomonas syringae pv. phaseolicola]. 323 22

Moraxella lacunata and Moraxella bovis use type 4 pili to adhere to epithelial tissues of the cornea and conjunctiva. Primer extension analyses were used to map the transcriptional start sites for the genes encoding the major pilin subunits (tfpQ/I) and the DNA invertase (piv), which determines pilin type expression. tfpQ/I transcription starts at a sigma54-dependent promoter (tfpQ/Ip2) and, under certain growth conditions, this transcription is accompanied by weaker upstream transcription that starts at a potential sigma70-dependent promoter (tfpQ/Ip1). piv is expressed in both M. lacunata and M. bovis from a putative sigma70-dependent promoter (pivp) under all conditions assayed. Sigma54-dependent promoters require activators in order to initiate transcription; therefore, it is likely that tfpQ/Ip2 is also regulated by an activator in Moraxella. Primer extension assays with RNA isolated from Escherichia coli containing the subcloned pilin inversion region from M. lacunata showed that pivp is used for the expression of piv; however, tfpQ/Ip2 is not used for the transcription of tfpQ/I. Transcription from tfpQ/Ip2 was activated in E. coli when the sensor (PilS) and response regulator (PilR) proteins of type 4 pilin transcription in Pseudomonas aeruginosa were expressed from a plasmid. These results suggest that the expression of the type 4 pilin in M. lacunata and M. bovis is regulated not only by a site-specific DNA inversion system but also by a regulatory system which is functionally analogous to the PilS-PilR two-component system of P. aeruginosa.
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PMID:Transcriptional regulation of type 4 pilin genes and the site-specific recombinase gene, piv, in Moraxella lacunata and Moraxella bovis. 939 93

The haloalkane-degrading bacteria Rhodococcus rhodochrous NCIMB13064, Pseudomonas pavonaceae 170, and Mycobacterium sp. strain GP1 share a highly conserved haloalkane dehalogenase gene (dhaA). Here, we describe the extent of the conserved dhaA segments in these three phylogenetically distinct bacteria and an analysis of their flanking sequences. The dhaA gene of the 1-chlorobutane-degrading strain NCIMB13064 was found to reside within a 1-chlorobutane catabolic gene cluster, which also encodes a putative invertase (invA), a regulatory protein (dhaR), an alcohol dehydrogenase (adhA), and an aldehyde dehydrogenase (aldA). The latter two enzymes may catalyze the oxidative conversion of n-butanol, the hydrolytic product of 1-chlorobutane, to n-butyric acid, a growth substrate for many bacteria. The activity of the dhaR gene product was analyzed in Pseudomonas sp. strain GJ1, in which it appeared to function as a repressor of dhaA expression. The 1,2-dibromoethane-degrading strain GP1 contained a conserved DNA segment of 2.7 kb, which included dhaR, dhaA, and part of invA. A 12-nucleotide deletion in dhaR led to constitutive expression of dhaA in strain GP1, in contrast to the inducible expression of dhaA in strain NCIMB13064. The 1, 3-dichloropropene-degrading strain 170 possessed a conserved DNA segment of 1.3 kb harboring little more than the coding region of the dhaA gene. In strains 170 and GP1, a putative integrase gene was found next to the conserved dhaA segment, which suggests that integration events were responsible for the acquisition of these DNA segments. The data indicate that horizontal gene transfer and integrase-dependent gene acquisition were the key mechanisms for the evolution of catabolic pathways for the man-made chemicals 1, 3-dichloropropene and 1,2-dibromoethane.
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PMID:Roles of horizontal gene transfer and gene integration in evolution of 1,3-dichloropropene- and 1,2-dibromoethane-degradative pathways. 1073 62

The relatively unknown, non-pathogenic, dimorphic, haploid, ascomycetous yeast Arxula adeninivorans exhibits some unusual properties which are of biotechnological interest. The yeast is able to assimilate and ferment many compounds as sole source of carbon and/or nitrogen, it utilises n-alkanes and degrades starch efficiently. A. adeninivorans features such as thermo- and haloresistance as well as the yeast's uncommon growth and secretion behaviour should be especially emphasised. In media containing up to 20% NaCl, A. adeninivorans is able to grow at cultivation temperatures up to 48 degrees C. Additionally, the dimorphism of the yeast is unusual. Arxula grows at up temperatures of up to 42 degrees C as budding cells, which turn into mycelia at higher temperatures. This environmentally conditioned dimorphism is reversible and budding is reestablished when the cultivation temperature is decreased below 42 degrees C. Alteration of morphology correlates with changes in secretion behaviour. Mycelium cultures accumulate two-fold higher protein concentrations and contain two- to five-fold higher glucoamylase and invertase activities in the medium than budding cells. Based on these unusual properties, Arxula adeninivorans is used for heterologous gene expression and as a gene donor to construct more suitable yeasts for biotechnology. For example the Arxula glucoamylase gene was successfully expressed in Saccharomyces cerevisiae and Kluyveromyces lactis. Both transformed yeasts are able to assimilate and ferment starch as carbon source. A transformation system is used for heterologous gene expression which is based on integration of linearised DNA fragments in two to ten copies, e.g. into the 25S rDNA of A. adeninivorans by homologous recombination. The obtained transformants are mitotically stable. The expression of the lacZ gene from E. coli as well as the XylE gene from Pseudomonas putida indicates the suitability of A. adeninivorans as host for heterologous gene expression.
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PMID:Genetic transformation and biotechnological application of the yeast Arxula adeninivorans. 1113 85

The invertase inhibitory protein isolated from Cyphomandra betacea Sendt and Solanum tuberosum inhibited the invertase activity from different species, genera and even plant family. Furthermore, proteinaceous inhibitors are not invertase specific; fungal, bacterial and higher plant enzymes including polygalacturonase, pectinase, pectin lyase, alpha-L-arabinofuranosidase and beta-glucosidase are also shown to be inhibited. Both inhibitors exhibited an in vitro antibacterial action against phytopathogenics strains of Xanthomonas campestris pvar vesicatoria CECT 792, Pseudomonas solanacearum CECT 125, Pseudomonas corrugata CECT 124, Pseudomonas syringae and Erwinia carotovora var carotovora.
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PMID:Inhibition of hydrolytic enzyme activities and plant pathogen growth by invertase inhibitors. 1236 59

Broad-spectrum antimicrobial activity of an invertase inhibitory protein (IIP) isolated from Cyphomandra betacea ripe fruits is documented. Minimal inhibitory concentration (MIC) values were determined by agar macrodilution and broth microdilution assays. This IIP inhibited the growth of xylophagous and phytopatogenic fungi (Ganoderma applanatum, Schizophyllum commune, Lenzites elegans, Pycnoporus sanguineous, Penicillium notatum, Aspergillus niger, Phomopsis sojae and Fusarium mango) and phytopathogenic bacteria (Xanthomonas campestris pvar vesicatoria CECT 792, Pseudomonas solanacearum CECT 125, Pseudomonas corrugata CECT 124, Pseudomonas syringae pv. syringae and Erwinia carotovora var carotovora). The IIP concentration required to completely inhibit the growth of all studied fungi ranged from 7.8 to 62.5 microg/ml. Phytopatogenic bacteria were the most sensitive, with MIC values between 7.8 and 31.25 microg/ml. Antifungal and antibacterial activities can be associated with their ability to inhibit hydrolytic enzymes. Our results indicate the possible participation of IIP in the plant defense mechanism and its potential application as a biocontrol agent against phytopathogenic fungi and bacteria.
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PMID:Antimicrobial activity of glycosidase inhibitory protein isolated from Cyphomandra betacea Sendt. fruit. 1640 43

ABSTRACT Forty bacterial strains isolated from leek blight (Allium porrum) in France and other countries were studied by conventional biochemical methods, serological reactions, numerical taxonomy, DNA-DNA hybridization, and ice nucleation activity, as well as by pathogenicity on leek and other host plants. They were compared with reference strains of Pseudomonas, mainly pathotype strains of P. syringae pathovars and strains of P. syringae pv. syringae isolated from various host plants including onions. Leek strains sorted with P. syringae species (sensu lato) by LOPAT tests (production of levan-sucrase, oxidase, pectinase, arginine dihydrolase, and hypersensitive reaction on tobacco). Leek strains were pathogenic to leek and produced symptoms identical to those observed in the field. They were the only strains in our study that could cause blight of leek. Thus, our results justify the creation of a new pathovar. Leek strains constituted a highly homogeneous DNA group and a discrete phenon by numerical taxonomy, and they belonged to O-serogroup POR. The name of P. syringae pv. porri is proposed for the bacterium causing leek blight. Criteria for routine identification are presented and taxonomic status is discussed.
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PMID:Description of the Bacterium Causing Blight of Leek as Pseudomonas syringae pv. porri (pv. nov.). 1894 92

Fifty-four Pectobacterium carotovorum subsp. carotovorum strains isolated in Korea were characterized by a spectrum of antibacterial activities against 7 indicator strains chosen to represent various regions and host plants. All P. carotovorum subsp. carotovorum isolates tested could be grouped into 4 classes depending on the pattern of antibacterial substance production. All tested strains had DNA fragment(s) homologous to the genes encoding carotovoricin and 21 of them had genes homologous to DNA invertase. Sixteen strains had genes homologous to the genes encoding carocin S1. Several isolates produced antibacterial substances active against strains in Brenneria, Pantoea, and Pectobacterium genera that belonged formerly to the genus Erwinia. Strains in Pseudomonas or Xanthomonas sp. were not sensitive to the antibacterial substances produced by P. carotovorum subsp. carotovorum, except for X. albilineans that was sensitive to antibacterial substances produced by most strains in P. carotovorum subsp. carotovorum and P. betavasculorum KACC10056. These results demonstrated the diverse patterns of antibacterial substance production and the possibility of the existence of new antibacterial substance(s) produced by P. carotovorum subsp. carotovorum isolated in Korea.
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PMID:Diverse Antibacterial activity of Pectobacterium carotovorum subsp.carotovorum isolated in Korea. 1919 Apr 7

There is increasing evidence that pathogens do not only elicit direct defense responses, but also cause pronounced changes in primary carbohydrate metabolism. Cell-wall-bound invertases belong to the key regulators of carbohydrate partitioning and source-sink relations. Whereas studies have focused so far only on the transcriptional induction of invertase genes in response to pathogen infection, the role of post-translational regulation of invertase activity has been neglected and was the focus of the present study. Expression analyses revealed that the high mRNA level of one out of three proteinaceous invertase inhibitors in source leaves of Arabidopsis thaliana is strongly repressed upon infection by a virulent strain of Pseudomonas syringae pv. tomato DC3000. This repression is paralleled by a decrease in invertase inhibitor activity. The physiological role of this regulatory mechanism is revealed by the finding that in situ invertase activity was detectable only upon infection by P. syringae. In contrast, a high invertase activity could be measured in vitro in crude and cell wall extracts prepared from both infected and non-infected leaves. The discrepancy between the in situ and in vitro invertase activity of control leaves and the high in situ invertase activity in infected leaves can be explained by the pathogen-dependent repression of invertase inhibitor expression and a concomitant reduction in invertase inhibitor activity. The functional importance of the release of invertase from post-translational inhibition for the defense response was substantiated by the application of the competitive chemical invertase inhibitor acarbose. Post-translational inhibition of extracellular invertase activity by infiltration of acarbose in leaves was shown to increase the susceptibility to P. syringae. The impact of invertase inhibition on spatial and temporal dynamics of the repression of photosynthesis and promotion of bacterial growth during pathogen infection supports a role for extracellular invertase in plant defense. The acarbose-mediated increase in susceptibility was also detectable in sid2 and cpr6 mutants and resulted in slightly elevated levels of salicylic acid, demonstrating that the effect is independent of the salicylic acid-regulated defense pathway. These findings provide an explanation for high extractable invertase activity found in source leaves that is kept inhibited in situ by post-translational interaction between invertase and the invertase inhibitor proteins. Upon pathogen infection, the invertase activity is released by repression of invertase inhibitor expression, thus linking the local induction of sink strength to the plant defense response.
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PMID:Post-translational derepression of invertase activity in source leaves via down-regulation of invertase inhibitor expression is part of the plant defense response. 2083 35

The ecotoxicological effects of decabromodiphenyl ether (BDE209) and cadmium (Cd) contamination on soil culturable microbial population, enzyme activity and bacterial community structure were investigated. Results of the indoor incubation test runs performed on many series of control and contaminated soil samples have demonstrated some notable toxic effects due to long term exposure to either or both contaminants. The two contaminants produced notable yet different toxic effects on the test microbes; the population of the exposed species generally declined according to certain dose-response relationships. The soil culturable microbial population and enzyme activity data show that the sensitivity to one or both contaminants followed the order of: bacteria>fungi>actinomycete and urease>saccharase, respectively. The interaction between BDE209 and Cd was dependent on both the exposure dose and time and that the joint toxic effects were synergistic, antagonistic or additive. The PCR-DGGE analysis data of species composition and richness suggest the synergistic combined effects on bacterial community structure during the 30d exposure. Pseudomonas tuomuerensis strain CCM 7280 and Pseudomonas alcaliphila strain AL15-21 were enriched, indicating these species might be major functional populations and highly tolerant. Such observations have provided the useful information of potential ecotoxicological effects of BDE209 and Cd contamination in the environment.
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PMID:Ecotoxicological effects of decabromodiphenyl ether and cadmium contamination on soil microbes and enzymes. 2269 81


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