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salmonella infections/phosphatase
Ο σύνδεσμος αποθηκεύεται στο πρόχειρο
Σελίδα 1 από 368 Αποτελέσματα
Fluorometric Analysis of Alkaline Phosphatase Inactivation Correlated to Salmonella and Listeria Inactiviation.
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The correlation between alkaline phosphatase (ALP) inactivation and bacterial pathogen inactivation in raw milk was studied using a newly Association of Official Analytical Chemists-approved fluorometric assay (AOAC 991.24). Fresh, raw milk was inoculated with Listeria monocytogenes Scott A and
Periplasmic nonspecific acid phosphatase II from Salmonella typhimurium LT2. Crystallization, detergent reactivation, and phosphotransferase activity.
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The periplasmic nonspecific acid phosphatase II from Salmonella typhimurium was purified to homogeneity from a mutant strain that overproduces the enzyme (Uerkvitz, W., and Beck, C.F. (1981) J. Biol. Chem. 256, 382-389). It was shown that the enzyme transfers phosphate groups from organic phosphoric
Molecular analysis of the Salmonella typhimurium phoN gene, which encodes nonspecific acid phosphatase.
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The phoN gene of Salmonella typhimurium encodes nonspecific acid phosphatase (EC 3.1.3.2), which is regulated by a two-component regulatory system consisting of the phoP and phoQ genes. We cloned the phoN region into a plasmid vector by complementation of a phoN mutant strain and determined the
Structural Analysis of Binding Determinants of Salmonella typhimurium Trehalose-6-phosphate Phosphatase using Ground-State Complexes
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Trehalose-6-phosphate phosphatase (T6PP) catalyzes the dephosphorylation of trehalose 6-phosphate (T6P) to the disaccharide trehalose. The enzyme is not present in mammals but is essential to the viability of multiple lower organisms as trehalose is a critical metabolite and T6P accumulation is
The secreted Salmonella dublin phosphoinositide phosphatase, SopB, localizes to PtdIns(3)P-containing endosomes and perturbs normal endosome to lysosome trafficking.
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Invasion and survival in mammalian cells by Salmonella enterica is mediated by bacterial proteins that are delivered to the host cell cytoplasm by type III secretion systems. One of these proteins, SopB/SigD, is a phosphoinositide phosphatase that can hydrolyse a number of substrates in vitro
Role of tyrosine kinases and the tyrosine phosphatase SptP in the interaction of Salmonella with host cells.
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Salmonella has evolved an intimate functional interface with its host. Central to this interface is a battery of bacterial proteins delivered into host cells via a specialized organelle termed the type III secretion system. A subset of these bacterial proteins stimulates cellular responses by
PrpZ, a Salmonella enterica serovar Typhi serine/threonine protein phosphatase 2C with dual substrate specificity.
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Genes encoding eukaryotic-type protein kinases and phosphatases are present in many bacterial genomes. An ORF encoding a polypeptide with homology to protein phosphatases 2C (PP2Cs) was identified in the genomes of Salmonella enterica serovar Typhi strains CT18 and Ty2. This protein, termed PrpZ, is
The PPP-family protein phosphatases PrpA and PrpB of Salmonella enterica serovar Typhimurium possess distinct biochemical properties.
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Salmonella enterica serovar Typhimurium requires Mn(2+), but only a few Mn(2+)-dependent enzymes have been identified from bacteria. To characterize Mn(2+)-dependent enzymes from serovar Typhimurium, two putative PPP-family protein phosphatase genes were cloned from serovar Typhimurium and named
Repression of alkaline phosphatase in Salmonella typhimurium carrying a phoA+ phoR- episome from Escherichia coli.
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Salmonella typhimurium does not produce alkaline phosphatase (nor beta-galactosidase). Nevertheless, it has the function of the phoR+ regulatory gene but lacks the function of the lacI+ regulatory gene. Several periplasmic proteins are derepressed when cells of S. typhimurium are starved for
Phosphoprotein phosphatase activity associated with the cytoplasmic membrane of Salmonella typhimurium and Escherichia coli.
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Membrane-associated phosphoprotein phosphatase activity was demonstrated in extracts of Salmonella typhimurium and Escherichia coli. The active protein could be extracted from the membrane as a large water-soluble complex (Mr greater than 150,000). Maximal activity was observed at pH 6 to 7 in the
Bromoperoxidase activity of vanadate-substituted acid phosphatases from Shigella flexneri and Salmonella enterica ser. typhimurium.
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Vanadium haloperoxidases and the bacterial class A nonspecific acid phosphatases have a conserved active site. It is shown that vanadate-substituted recombinant acid phosphatase from Shigella flexneri (PhoN-Sf) and Salmonella enterica ser. typhimurium (PhoN-Se) in the presence of H2O2 are able to
The phosphatase activity is the target for Mg2+ regulation of the sensor protein PhoQ in Salmonella.
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The PhoP/PhoQ two-component system controls the expression of essential virulence traits in the pathogenic bacterium Salmonella enterica serovar Typhimurium. Environmental deprivation of Mg(2+) activates the PhoP/PhoQ signal transduction cascade, which results in an increased expression of genes
Physiological function of periplasmic hexose phosphatase in Salmonella typhimurium.
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Hydrolysis of sugar phosphates by crude and purified preparations of periplasmic hexose phosphatase from Salmonella typhimurium followed Michaelis-Menten kinetics. The enzyme bound glucose 1-phosphate with high affinity (Km = 10 microM) but bound glucose 6-phosphate with low affinity (Km = 2,000
The identification of distinct protein kinases and phosphatases in the prokaryote Salmonella typhimurium.
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The finding of protein phosphorylation in prokaryotes (Wang, J. Y. J., and Koshland, D. E. (1978) J. Biol. Chem. 253, 7605-7608) has been pursued further. The prokaryotic organism Salmonella typhimurium is shown to contain at least 10 phosphorylated proteins with serine or threonine phosphates which
Molecular characterization of the Salmonella typhi StpA protein that is related to both Yersinia YopE cytotoxin and YopH tyrosine phosphatase.
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Analysis of the nucleotide sequence of a 4-kb DNA fragment located between the sip and iag loci on Salmonella typhi chromosome revealed three open reading frames, termed sipF, ctpA and stpA. The 82-amino-acid (aa) sipF product showed extensive similarity to the lacP protein from S. typhimurium. The
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