Výsledky vyhledávání - "and Octavian Bârzu"

Borrelia burgdorferi uridine kinase: an enzyme of the pyrimidine salvage pathway for endogenous use of nucleotides

Autor: I. Saint Girons, A.M Gilles, Caroline Boursaux-Eude, Danielle Margarita, Octavian Bârzu

Publikováno v: FEMS Microbiology Letters. 151:257-261

The 621 bp udk gene encoding Borrelia burgdorferi potential uridine kinase, involved in the pyrimidine salvage pathway, was cloned and sequenced. The B. burgdorferi protein has a molecular mass of 24 kDa in sodium dodecyl sulfate-polyacrylamide gel.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b816cb9f842a08611a73bd18c9ce2003
https://doi.org/10.1111/j.1574-6968.1997.tb12579.x

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Insight into the activation mechanism of Bordetella pertussis adenylate cyclase by calmodulin using fluorescence spectroscopy

Autor: Hélène Munier-Lehmann, Inès Li de la Sierra, Michel Vincent, Anne-Marie Gilles, Madalena Renouard, Octavian Bârzu, Jacques Gallay, Hiroshi Sakamoto

Publikováno v: European Journal of Biochemistry. 271:821-833

The interaction of the adenylate cyclase catalytic domain (AC) of the Bordetella pertussis major exotoxin with its activator calmodulin (CaM) was studied by time-resolved fluorescence spectroscopy using three fluorescent groups located in different r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c5c040d393c9cf9589225c3d9e9982fc
https://doi.org/10.1111/j.1432-1033.2004.03987.x

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UMP kinase from the Gram-positive bacterium Bacillus subtilis is strongly dependent on GTP for optimal activity

Autor: Antoine Danchin, Cristina Gagyi, Nadia Bucurenci, Gilles Labesse, Liliane Assairi, Augustin Ofiteru, Ovidiu Sîrbu, Octavian Bârzu, Stéphanie Landais, Anne-Marie Gilles, Mihaela Ileana Ionescu

Publikováno v: European Journal of Biochemistry. 270:3196-3204

The gene encoding Bacillus subtilis UMP kinase (pyrH/smbA) is transcribed in vivo into a functional enzyme, which represents approximately 0.1% of total soluble proteins. The specific activity of the purified enzyme under optimal conditions is 25 uni

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e00d4b49961df975e658d325588a5b5e
https://doi.org/10.1046/j.1432-1033.2003.03702.x

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Sugar specificity of bacterial CMP kinases as revealed by crystal structures and mutagenesis of Escherichia coli enzyme

Autor: Pierre Briozzo, Thomas Bertrand, Augustin Ofiteru, Béatrice Golinelli-Pimpaneau, Nadia Bucurenci, Anne-Marie Gilles, Octavian Bârzu, Liliane Assairi, Hélène Munier-Lehmann

Publikováno v: Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2002, 315 (5), pp.1099-110. ⟨10.1006/jmbi.2001.5286⟩
Journal of Molecular Biology, 2002, 315 (5), pp.1099-110. ⟨10.1006/jmbi.2001.5286⟩

International audience; Bacterial cytidine monophosphate (CMP) kinases are characterised by an insert enlarging their CMP binding domain, and by their particular substrate specificity. Thus, both CMP and 2'-deoxy-CMP (dCMP) are good phosphate accepto

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32ac4d444cbef836fb829e8bc3e8aa96
https://doi.org/10.1006/jmbi.2001.5286

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Nanosecond Fluorescence Dynamic Stokes Shift of Tryptophan in a Protein Matrix

Autor: and Octavian Bârzu, ‡ Anne-Marie Gilles, Ines M. Li De La Sierra, Michel Vincent, Pierre Briozzo, Jacques Gallay

Publikováno v: The Journal of Physical Chemistry B. 104:11286-11295

The fluorescent dynamic Stokes shift (FDSS) method has emphasized a time-dependent dipolar relaxation process around the single tryptophan residue (Trp31) in cytidine monophosphate kinase from E. coli (CMPK). This Trp residue, located close to the pr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2909d2c1153f8c9fbe9f19ba8282fbb6
https://doi.org/10.1021/jp000638x

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Two-Dimensional Infrared Correlation Analysis of Protein Unfolding: Use of Spectral Simulations to Validate Structural Changes during Thermal Denaturation of Bacterial CMP Kinases

Autor: Christian P. Schultz, Octavian Bârzu, Henry H. Mantsch

Publikováno v: Applied Spectroscopy. 54:931-938

The functional role of bacterial CMP kinases is to recover the energetically exhausted nucleoside monophosphates derived from cell metabolism by transferring a phosphate residue from ATP to CMP or dCMP. These enzymes—important for cell growth and d

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3528e4ab7066b1974061fac95cef2cf2
https://doi.org/10.1366/0003702001950562

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Decreased Capacity of Recombinant 45/47-kDa Molecules (Apa) of Mycobacterium tuberculosis to Stimulate T Lymphocyte Responses Related to Changes in Their Mannosylation Pattern

Autor: Michel Rivière, Abdelkader Namane, Cynthia Horn, Germain Puzo, Felix Romain, Pascale Pescher, Octavian Bârzu, Gilles Marchal

Publikováno v: Journal of Biological Chemistry. 274:32023-32030

The Apa molecules secreted by Mycobacterium tuberculosis, Mycobacterium bovis, or BCG have been identified as major immunodominant antigens. Mass spectrometry analysis indicated similar mannosylation, a complete pattern from 1 up to 9 hexose residues

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::183b9908382fa8f15bf46e5e2fa7eb14
https://doi.org/10.1074/jbc.274.45.32023

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Autor: Elisabeth Carniel, Anne-Marie Gilles, Octavian Bârzu, Lise Tourneux, Petya Christova, Viviane Chenal-Francisque, Inès Li de la Sierra

Publikováno v: European Journal of Biochemistry. 265:112-119

Thymidine monophosphate (TMP) kinases are key enzymes in nucleotide synthesis for all living organisms. Although eukaryotic and viral TMP kinases have been studied extensively, little is known about their bacterial counterparts. To characterize the T

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41a57db6d039693a1d6fe8dd83652f47
https://doi.org/10.1046/j.1432-1327.1999.00691.x

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Multinuclear magnetic resonance studies of Escherichia coli adenylate kinase in free and bound forms . Resonance assignment, secondary structure and ligand binding

Autor: A. Popescu, Anne-Marie Gilles, Constantin T. Craescu, Octavian Bârzu, Simona Burlacu-Miron

Publikováno v: European Journal of Biochemistry. 264:765-774

The crystal structure of Escherichia coli adenylate kinase (AKe) revealed three main components: a CORE domain, composed of a five-stranded parallel beta-sheet surrounded by alpha-helices, and two peripheral domains involved in covering the ATP in th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3510eadbf446e7c99877d850934b666
https://doi.org/10.1046/j.1432-1327.1999.00633.x

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Characterization of Metal and Nucleotide Liganded Forms of Adenylate Kinase by Electrospray Ionization Mass Spectrometry

Autor: Masayuki Takahashi, Gilbert Briand, Octavian Bârzu, Véronique Perrier, Anne-Marie Gilles, Mostafa Kouach

Publikováno v: Archives of Biochemistry and Biophysics. 339:291-297

Complexes of adenylate kinase from Escherichia coli, Bacillus subtilis, and Bacillus stearothermophilus with the bisubstrate nucleotide analog P1,P5-di(adenosine 5')-pentaphosphate and with metal ions (Zn2+ and/or Mg2+) were analyzed by electrospray

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e40ea6552c4f23176d8c9b05cf4cce5c
https://doi.org/10.1006/abbi.1997.9877

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