Carbon catabolite repression in Bacillus subtilis: quantitative analysis of repression exerted by different carbon sources. - Wikidata - awgldk - TriplyDB

Carbon catabolite repression in Bacillus subtilis: quantitative analysis of repression exerted by different carbon sources.

Carbon catabolite repression in Bacillus subtilis: quantitative analysis of repression exerted by different carbon sources.

http://www.wikidata.org/entity/Q42011325

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Prediction of the mechanism of action of fusaricidin on Bacillus subtilis CcpA forms complexes with CodY and RpoA in Bacillus subtilis Crh, the paralogue of the phosphocarrier protein HPr, controls the methylglyoxal bypass of glycolysis in Bacillus subtilis High- and low-affinity cre boxes for CcpA binding in Bacillus subtilis revealed by genome-wide analysis Effect of a glucose impulse on the CcpA regulon in Staphylococcus aureus Metabolic fluxes during strong carbon catabolite repression by malate in Bacillus subtilis.Class IIa bacteriocin resistance in Enterococcus faecalis V583: the mannose PTS operon mediates global transcriptional responses Comparative transcriptome analysis of Bacillus subtilis responding to dissolved oxygen in adenosine fermentation CcpA ensures optimal metabolic fitness of Streptococcus pneumoniae.Regulation of CodY activity through modulation of intracellular branched-chain amino acid pools.Xylitol production from xylose mother liquor: a novel strategy that combines the use of recombinant Bacillus subtilis and Candida maltosa.Hierarchy in pentose sugar metabolism in Clostridium acetobutylicum Niche-specific contribution to streptococcal virulence of a MalR-regulated carbohydrate binding protein.Confirmation and elimination of xylose metabolism bottlenecks in glucose phosphoenolpyruvate-dependent phosphotransferase system-deficient Clostridium acetobutylicum for simultaneous utilization of glucose, xylose, and arabinose Malate-mediated carbon catabolite repression in Bacillus subtilis involves the HPrK/CcpA pathway.NanI Sialidase, CcpA, and CodY Work Together To Regulate Epsilon Toxin Production by Clostridium perfringens Type D Strain CN3718.Phosphoproteome dynamics mediate revival of bacterial spores Two enzymes with redundant fructose bisphosphatase activity sustain gluconeogenesis and virulence in Mycobacterium tuberculosis.The phosphoenolpyruvate:sugar phosphotransferase system is involved in sensitivity to the glucosylated bacteriocin sublancin.A novel mode of regulation of the Staphylococcus aureus catabolite control protein A (CcpA) mediated by Stk1 protein phosphorylation Catabolite control protein E (CcpE) is a LysR-type transcriptional regulator of tricarboxylic acid cycle activity in Staphylococcus aureus.Carbon catabolite repression in Pseudomonas : optimizing metabolic versatility and interactions with the environment.Coordination of microbial metabolism.Overproduction of Bacillus amyloliquefaciens extracellular glutamyl-endopeptidase as a result of ectopic multi-copy insertion of an efficiently-expressed mpr gene into the Bacillus subtilis chromosome Research Progress Concerning Fungal and Bacterial β-Xylosidases.Characterization and regulation of a bacterial sugar phosphatase of the haloalkanoate dehalogenase superfamily, AraL, from Bacillus subtilis.Probing the regulatory effects of specific mutations in three major binding domains of the pleiotropic regulator CcpA of Bacillus subtilis In vitro imaging of bacteria using 18F-fluorodeoxyglucose micro positron emission tomography.From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later.An Alternative Bacterial Expression System Using Bacillus pumilus SG2 Chitinase Promoter.Prevention of cross-talk in conserved regulatory systems: identification of specificity determinants in RNA-binding anti-termination proteins of the BglG family.Determinants of interaction specificity of the Bacillus subtilis GlcT antitermination protein: functionality and phosphorylation specificity depend on the arrangement of the regulatory domains.Carbon catabolite repression in Thermoanaerobacterium saccharolyticum.Malate metabolism in Bacillus subtilis: distinct roles for three classes of malate-oxidizing enzymes.Adaptation of Bacillus subtilis carbon core metabolism to simultaneous nutrient limitation and osmotic challenge: a multi-omics perspective.The MsmX ATPase plays a crucial role in pectin mobilization by Bacillus subtilis.GH115 α-glucuronidase and GH11 xylanase from Paenibacillus sp. JDR-2: potential roles in processing glucuronoxylans.Impact of Seed Exudates on Growth and Biofilm Formation of Bacillus amyloliquefaciens ALB629 in Common Bean.L-Proline nutrition and catabolism in Staphylococcus saprophyticus.Diauxic growth of Clostridium acetobutylicum ATCC 824 when grown on mixtures of glucose and cellobiose.

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Carbon catabolite repression in Bacillus subtilis: quantitative analysis of repression exerted by different carbon sources.

http://www.wikidata.org/entity/Q42011325

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2008 nî lūn-bûn

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Carbon catabolite repression i ...... d by different carbon sources.

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Carbon catabolite repression i ...... d by different carbon sources.

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Kalpana D Singh

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Matthias H Schmalisch

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P2860

Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria

Structural mechanism for the fine-tuning of CcpA function by the small molecule effectors glucose 6-phosphate and fructose 1,6-bisphosphate

Mutations lowering the phosphatase activity of HPr kinase/phosphatase switch off carbon metabolism

SPINE: a method for the rapid detection and analysis of protein-protein interactions in vivo

Loss of protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, by mutation of the ptsH gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis

Carbon catabolite repression in bacteria: many ways to make the most out of nutrients

Mechanistic and physiological consequences of HPr(ser) phosphorylation on the activities of the phosphoenolpyruvate:sugar phosphotransferase system in gram-positive bacteria: studies with site-specific mutants of HPr.

The HPr kinase from Bacillus subtilis is a homo-oligomeric enzyme which exhibits strong positive cooperativity for nucleotide and fructose 1,6-bisphosphate binding.

Phosphorylation of HPr and Crh by HprK, early steps in the catabolite repression signalling pathway for the Bacillus subtilis levanase operon.

Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors.

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