Výsledky vyhledávání

Structures of mutants of cellulase Ce148F of Clostridium cellulolyticum in complex with long hemithiocellooligosaccharides give rise to a new view of the substrate pathway during processive action

Autor: Parsiegla, G., Reverbel, C., Tardif, C., Driguez, H., Haser, R.

Publikováno v: Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2008, 375, pp.499-510

International audience; An efficient breakdown of lignocellulosic biomass is a prerequisite for the production of second-generation biofuels. Cellulases are key enzymes in this process. We crystallized complexes between hemithio-cello-deca and dodeca

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::a4b1c2563bf7d7f709620ba336f975fb
https://hal.archives-ouvertes.fr/hal-00315186

Zobrazit plný text záznamu

Insights into sucrose isomerization from crystal structures of the Pseudomonas mesoacidophila MX-45 sucrose isomerase, MutB

Autor: Ravaud, S., Robert, X., Watzlawick, H., Laurent, S., Haser, R., Mattes, R., Nushin Aghajari

Publikováno v: Biocatalysis and Biotransformation
Biocatalysis and Biotransformation, Taylor & Francis, 2008, 26, pp.111-119
HAL

International audience; Three-dimensional structures of a sucrose isomerase from Pseudomonas mesoacidophila MX-45, forming mainly trehalulose have been solved to resolutions in the range 1.8-2.2 angstrom . Native and mutant complexes give, for the fi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::89007fc3ad887613d4e7db6af1441b80
https://hal.archives-ouvertes.fr/hal-00315188

Zobrazit plný text záznamu

Etude structurale de mutants d’integrases rétrovirales

Autor: Ballandras, A, Moreau, Karen, Gallay, Kathy, Haser, R, Ronfort, Corinne, Gouet, P

Publikováno v: GTBio
GTBio, 2007, Lille, France. pp.Inconnu, 2007

National audience

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::38ff5c09a6e11de70836f250f53185d5
https://hal.inrae.fr/hal-02823477

Zobrazit plný text záznamu

The 'pair of sugar tongs' site on the non-catalytic domain C of barley alpha-amylase participates in substrate binding and activity

Autor: Bozonnet, S., Mt Jensen, Mm Nielsen, Nushin Aghajari, Mh Jensen, Kramhoft, B., Willemoes, M., Tranier, S., Haser, R., Svensson, B.

Publikováno v: FEBS Journal
FEBS Journal, Wiley, 2007, xxx, pp.5055-5067
Technical University of Denmark Orbit
HAL

International audience; Some starch-degrading enzymes accommodate carbohydrates at sites situated at a certain distance from the active site. In the crystal structure of barley alpha-amylase 1, oligosaccharide is thus bound to the 'sugar tongs' site.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::316cbe64481c60ec719891ca5c2ca90a
https://hal.archives-ouvertes.fr/hal-00315129

Zobrazit plný text záznamu

Structure of a d(TGGGGT) quadruplex crystallized in the presence of Li(+) ions

Autor: Creze, C., Rinaldi, B., Haser, R., Bouvet, Philippe, Gouet, P.

Publikováno v: Acta crystallographica Section D : Structural biology [1993-...]
Acta crystallographica Section D : Structural biology [1993-..], 2007, 63 (Pt 6), pp.682-688

International audience

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3393::fb9c5d2a307bb7c6c3abd3e00f26f95c
https://hal.science/hal-00337638

Zobrazit plný text záznamu

Oligosaccharide binding to barley alpha-amylase 1

Autor: Robert, X., Haser, R., Mori, H., Svensson, B., Nushin Aghajari

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2005, 280, pp.32968-32978
HAL

International audience; Enzymatic subsite mapping earlier predicted 10 binding subsites in the active site substrate binding cleft of barley alpha-amylase isozymes. The three-dimensional structures of the oligosaccharide complexes with barley alpha-a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::429d279ae91e6b655c440314b8f78332
https://hal.archives-ouvertes.fr/hal-00313533

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání