Výsledky vyhledávání - "Mycobacterium tuberculosis/enzymology"

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New substrates and interactors of the mycobacterial Serine/Threonine protein kinase PknG identified by a tailored interactomic approach

Autor: Roland Brosch, María Noel Alvarez, Mariana Piuri, Alessandro Cascioferro, Analía Lima, Rosario Durán, Paulo C. Carvalho, Estefanía Urdániz, María-Natalia Lisa, Ana Denicola, Marco Bellinzoni, Otto Pritsch, Federico Carrion, Magdalena Gil, Annemarie Wehenkel, Pedro M. Alzari, Carlos Batthyány, Bernardina Rivera, Jessica Rossello

Publikováno v: Journal of Proteomics
Journal of Proteomics, Elsevier, 2019, 192, pp.321-333. ⟨10.1016/j.jprot.2018.09.013⟩
Journal of Proteomics, 2019, 192, pp.321-333. ⟨10.1016/j.jprot.2018.09.013⟩

International audience; PknG from Mycobacterium tuberculosis is a multidomain Serine/Threonine protein kinase that regulates bacterial metabolism as well as the pathogen's ability to survive inside the host by still uncertain mechanisms. To uncover P

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48d6e591b08630f1c8a11067058c5008
https://hal-pasteur.archives-ouvertes.fr/pasteur-02046106

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QM/MM simulations identify the determinants of catalytic activity differences between type II dehydroquinase enzymes

Autor: Marc W. van der Kamp, Concepción González-Bello, Adrian J. Mulholland, Emilio Lence

Publikováno v: Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
instname
Minerva: Repositorio Institucional de la Universidad de Santiago de Compostela
Universidad de Santiago de Compostela (USC)
Lence, E, van der Kamp, M W, González-Bello, C & Mulholland, A J 2018, ' QM/MM simulations identify the determinants of catalytic activity differences between type II dehydroquinase enzymes ', Organic and Biomolecular Chemistry, vol. 16, no. 24, pp. 4443-4455 . https://doi.org/10.1039/C8OB00066B
Organic & Biomolecular Chemistry

Multiscale simulations pinpoint specific interactions responsible for differences in stabilization of key reacting species in two recognized targets for antibiotic development.
Type II dehydroquinase enzymes (DHQ2), recognized targets for antibi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0bc81c19cd3197e4365ac5bb4440f0dc
http://hdl.handle.net/10347/24328

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Metal-Ion Effects on the Polarization of Metal-Bound Water and Infrared Vibrational Modes of the Coordinated Metal Center of Mycobacterium tuberculosis Pyrazinamidase via Quantum Mechanical Calculations

Autor: Patricia Sheen, Melvin Orihuela, Jorge M. Seminario, Jimy J. Encomendero-Risco, Mirko Zimic, Karim Salazar-Salinas, Pedro A. Baldera-Aguayo

Publikováno v: The Journal of Physical Chemistry. B

Mycobacterium tuberculosis pyrazinamidase (PZAse) is a key enzyme to activate the pro-drug pyrazinamide (PZA). PZAse is a metalloenzyme that coordinates in vitro different divalent metal cofactors in the metal coordination site (MCS). Several metals

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c59aa255db261ddf1218085da8adb7f7
http://europepmc.org/articles/PMC4514207

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Identification and Mutagenesis by Allelic Exchange of choE , Encoding a Cholesterol Oxidase from the Intracellular Pathogen Rhodococcus equi

Autor: Jesús Navas, Néstor Ladrón, Bruno Gonzalez-Zorn, P. Garrido, José A. Vázquez-Boland

Publikováno v: Navas, J, González Zörn, B, Ladron, N, Garrido, P & Vazquez-Boland, J A 2001, ' Identification and mutagenesis by allelic exchange of choE, encoding a cholesterol oxidase from the intracellular pathogen Rhodococcus equi ', Journal of Bacteriology, vol. 183, no. 16, pp. 4796-805 . https://doi.org/10.1128/JB.183.16.4796-4805.2001

The nocardioform actinomycete Rhodococcus equi is a primary pathogen of horses. Rhodococcal infection occurs in foals aged under 6 months old and results in severe pyogranulomatous bronchopneumonia and a high mortality rate. Respiratory disease is so

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d269ce459072e528c86bb118996baa5
https://doi.org/10.1128/jb.183.16.4796-4805.2001

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