Výsledky vyhledávání - "Roswitha Engelmann"

Structure of the Full-length Enzyme I of the Phosphoenolpyruvate-dependent Sugar Phosphotransferase System

Autor: Klaus Scheffzek, Stefan Reinelt, Roswitha Engelmann, Wolfgang Hengstenberg, José A. Márquez, Brigitte Koch

Publikováno v: Journal of Biological Chemistry. 281:32508-32515

Enzyme I (EI) is the phosphoenolpyruvate (PEP)-protein phosphotransferase at the entry point of the PEP-dependent sugar phosphotransferase system, which catalyzes carbohydrate uptake into bacterial cells. In the first step of this pathway EI phosphor

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de8b6fba81c987d40ca1c6421aa88433
https://doi.org/10.1074/jbc.m513721200

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Expression of the Xylulose 5-Phosphate Phosphoketolase Gene, xpkA , from Lactobacillus pentosus MD363 Is Induced by Sugars That Are Fermented via the Phosphoketolase Pathway and Is Repressed by Glucose Mediated by CcpA and the Mannose Phosphoenolpyruvate Phosphotransferase System

Autor: Peter H. Pouwels, Pieter W. Postma, Clara C. Posthuma, Wolfgang Hengstenberg, Roswitha Engelmann, Rechien Bader

Publikováno v: Applied and Environmental Microbiology. 68:831-837

Purification of xylulose 5-phosphate phosphoketolase (XpkA), the central enzyme of the phosphoketolase pathway (PKP) in lactic acid bacteria, and cloning and sequence analysis of the encoding gene, xpkA , from Lactobacillus pentosus MD363 are describ

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4b390b12ccd47d706f530298a3d1736a
https://doi.org/10.1128/aem.68.2.831-837.2002

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The 1.9 Å resolution structure of phospho-serine 46 HPr from Enterococcus faecalis 1 1Edited by P. Wright

Autor: J. Wilson Quail, Koto Hayakawa, Louis T. J. Delbaere, Roswitha Engelmann, Wolfgang Hengstenberg, Josef Deutscher, Gerald F. Audette

Publikováno v: Journal of Molecular Biology. 303:545-553

The histidine-containing phosphocarrier protein HPr is a central component of the phosphoenolpyruvate:sugar phosphotransferase system (PTS), which transfers metabolic carbohydrates across the cell membrane in many bacterial species. In Gram-positive

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::cf596626acada4af4a57a9a1322f8054
https://doi.org/10.1006/jmbi.2000.4166

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Expression of the xylulose 5-phosphate phosphoketolase gene, xpkA, from Lactobacillus pentosus MD363 is induced by sugars that are fermented via the phosphoketolase pathway and is repressed by glucose mediated by CcpA and the mannose phosphoenolpyruvate phosphotransferase system

Autor: Clara C, Posthuma, Rechien, Bader, Roswitha, Engelmann, Pieter W, Postma, Wolfgang, Hengstenberg, Peter H, Pouwels

Publikováno v: Applied and environmental microbiology. 68(2)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b0a80394e8b1b800c86de1ee839bc4cf
https://pubmed.ncbi.nlm.nih.gov/11823225

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The hprK gene of Enterococcus faecalis encodes a novel bifunctional enzyme: The HPr kinase/phosphatase

Autor: Martin Blüggel, Roswitha Engelmann, Valérie Dossonnet, Josef Deutscher, Helmut E. Meyer, Melanie Kravanja, Anne Galinier, Rainer Frank, Norbert Friedemann Schnell, Wolfgang Hengstenberg

Publikováno v: Molecular Microbiology
Molecular Microbiology, Wiley, 1999, 31 (1), pp.59-66
Molecular Microbiology, Wiley, 1999, 31 (1), pp.59-66. ⟨10.1046/j.1365-2958.1999.01146.x⟩

Zeneca Pharmaceuticals, Mereside, Alderley Park,Macclesﬁeld, Cheshire SK10 4TG, UK.SummaryThe HPr kinase of Gram-positive bacteria is an ATP-dependent serine protein kinase, which phosphory-latesthe HPrprotein of the bacterial phosphotransfer-ase s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d1f629fded6b94fd01994bada25b2f7
https://hal.inrae.fr/hal-02697065

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New protein kinase and protein phosphatase families mediate signal transduction in bacterial catabolite repression

Autor: Jacques Haiech, Anne Galinier, Roswitha Engelmann, Marie-Claude Kilhoffer, Josef Deutscher, Melanie Kravanja, Wolfgang Hengstenberg

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 1998, 95 (4), pp.1823-1828. ⟨10.1073/pnas.95.4.1823⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 1998, 95 (4), pp.1823-1828

Carbon catabolite repression (CCR) is the prototype of a signal transduction mechanism. In enteric bacteria, cAMP was considered to be the second messenger in CCR by playing a role reminiscent of its actions in eukaryotic cells. However, recent resul

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36bdc8d5acb015de95f657404c9ed2af
https://hal.archives-ouvertes.fr/hal-02344558

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The structure of enzyme IIAlactose from Lactococcus lactis reveals a new fold and points to possible interactions of a multicomponent system

Autor: Emil F. Pai, Piotr Sliz, Wolfgang Hengstenberg, Roswitha Engelmann

Publikováno v: Scopus-Elsevier

Background: The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is responsible for the binding, transmembrane transport and phosphorylation of numerous sugar substrates. The system is also involved in the regulation of a variety

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40f0c0341a11f7636128adacf040447e
https://pubmed.ncbi.nlm.nih.gov/9261069

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