Pyrophosphate-producing protein dephosphorylation by HPr kinase/phosphorylase: a relic of early life? - Wikidata - awgldk - TriplyDB

Pyrophosphate-producing protein dephosphorylation by HPr kinase/phosphorylase: a relic of early life?

Pyrophosphate-producing protein dephosphorylation by HPr kinase/phosphorylase: a relic of early life?

http://www.wikidata.org/entity/Q34159595

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X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr Structural analysis of the bacterial HPr kinase/phosphorylase V267F mutant gives insights into the allosteric regulation mechanism of this bifunctional enzyme Structural Basis for the Regulation Mechanism of the Tyrosine Kinase CapB from Staphylococcus aureus Structural Characterizations of Glycerol Kinase: Unraveling Phosphorylation-Induced Long-Range Activation †Functional characterization of the incomplete phosphotransferase system (PTS) of the intracellular pathogen Brucella melitensis CcpA regulates arginine biosynthesis in Staphylococcus aureus through repression of proline catabolism Crh, the paralogue of the phosphocarrier protein HPr, controls the methylglyoxal bypass of glycolysis in Bacillus subtilis HPrK regulates succinate-mediated catabolite repression in the gram-negative symbiont Sinorhizobium meliloti Global analysis of carbohydrate utilization by Lactobacillus acidophilus using cDNA microarrays Elaborate transcription regulation of the Bacillus subtilis ilv-leu operon involved in the biosynthesis of branched-chain amino acids through global regulators of CcpA, CodY and TnrA.In vitro characterization of the Bacillus subtilis protein tyrosine phosphatase YwqE Reconstruction and analysis of the genetic and metabolic regulatory networks of the central metabolism of Bacillus subtilis.The bacterial phosphoenolpyruvate:carbohydrate phosphotransferase system: regulation by protein phosphorylation and phosphorylation-dependent protein-protein interactions.Low-molecular-weight protein tyrosine phosphatases of Bacillus subtilis.CcpA mediates proline auxotrophy and is required for Staphylococcus aureus pathogenesis Comparative genomic analyses of the bacterial phosphotransferase system.Role of phosphate in the central metabolism of two lactic acid bacteria--a comparative systems biology approach.Ser/Thr/Tyr protein phosphorylation in bacteria - for long time neglected, now well established.Overexpression of PrfA leads to growth inhibition of Listeria monocytogenes in glucose-containing culture media by interfering with glucose uptake CcpA-dependent carbon catabolite repression in bacteria.Protein-tyrosine phosphorylation in Bacillus subtilis: a 10-year retrospective.Malate-mediated carbon catabolite repression in Bacillus subtilis involves the HPrK/CcpA pathway.Inducer-modulated cooperative binding of the tetrameric CggR repressor to operator DNA How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria The phosphotransferase system of Lactobacillus casei: regulation of carbon metabolism and connection to cold shock response.Regulation of sugar catabolism in Lactococcus lactis.Regulation of transcription by eukaryotic-like serine-threonine kinases and phosphatases in Gram-positive bacterial pathogens.Metabolic Regulation of a Bacterial Cell System with Emphasis on Escherichia coli Metabolism.Research Progress Concerning Fungal and Bacterial β-Xylosidases.Exploring the diversity of protein modifications: special bacterial phosphorylation systems.Intertwining nutrient-sensory networks and the control of antibiotic production in Streptomyces.Sinorhizobium meliloti mutants lacking phosphotransferase system enzyme HPr or EIIA are altered in diverse processes, including carbon metabolism, cobalt requirements, and succinoglycan production.HPr kinase/phosphorylase, the sensor enzyme of catabolite repression in Gram-positive bacteria: structural aspects of the enzyme and the complex with its protein substrate High-resolution structure of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus aureus and characterization of its interaction with the bifunctional HPr kinase/phosphorylase.The phosphocarrier protein HPr of Neisseria meningitidis interacts with the transcription regulator CrgA and its deletion affects capsule production, cell adhesion, and virulence.The Lactobacillus casei ptsHI47T mutation causes overexpression of a LevR-regulated but RpoN-independent operon encoding a mannose class phosphotransferase system.Biophysical regulation of lipid biosynthesis in the plasma membrane.Carbon catabolite repression in Bacillus subtilis: quantitative analysis of repression exerted by different carbon sources.Carbon catabolite repression in Thermoanaerobacterium saccharolyticum.A eukaryotic type serine/threonine kinase and phosphatase in Streptococcus agalactiae reversibly phosphorylate an inorganic pyrophosphatase and affect growth, cell segregation, and virulence.

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P2860

Pyrophosphate-producing protein dephosphorylation by HPr kinase/phosphorylase: a relic of early life?

http://www.wikidata.org/entity/Q34159595

description

2002 nî lūn-bûn

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2002 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2002 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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Pyrophosphate-producing protei ...... rylase: a relic of early life?

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Pyrophosphate-producing protei ...... rylase: a relic of early life?

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Pyrophosphate-producing protei ...... rylase: a relic of early life?

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Pyrophosphate-producing protei ...... rylase: a relic of early life?

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Pyrophosphate-producing protei ...... rylase: a relic of early life?

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Pyrophosphate-producing protei ...... rylase: a relic of early life?

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Pyrophosphate-producing protei ...... rylase: a relic of early life?

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Pyrophosphate-producing protei ...... rylase: a relic of early life?

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Proceedings of the National Academy of Sciences of the United States of America

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Pyrophosphate-producing protei ...... rylase: a relic of early life?

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Anne Galinier

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Ivan Mijakovic

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José Antonio Marquez

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Klaus Scheffzek

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Sandrine Poncet

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Sonia Fieulaine

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Sonja Hasenbein

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Sylvie Nessler

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Wolfgang Hengstenberg

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P2860

Structure of the full-length HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 A resolution: Mimicking the product/substrate of the phospho transfer reactions.

X-ray structure of HPr kinase: a bacterial protein kinase with a P-loop nucleotide-binding domain

Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria

An aminoacyl-tRNA synthetase paralog with a catalytic role in histidine biosynthesis

X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr

The P-loop--a common motif in ATP- and GTP-binding proteins

Phosphoenolpyruvate carboxytransphosphorylase. II. Crystallization and properties

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

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

A new family of phosphotransferases with a P-loop motif.

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13442-13447

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10.1073/PNAS.212410399

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21

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99

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Vicente Monedero

Josef Deutscher

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2002-10-01T00:00:00Z

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11097618

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12359880

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129692

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