Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Birte Kramhøft"'
Autor:
Birte Svensson, Sophie Bozonnet, Martin Willemoës, Birte Kramhøft, Maher Abou Hachem, J. Nielsen, Susan L. S. Stipp
Publikováno v:
Archives of Biochemistry and Biophysics. 528:1-6
Barley α-amylase isozyme 1 (AMY1, EC 3.2.1.1) contains two surface binding sites, SBS1 and SBS2, involved in the degradation of starch granules. The distinct role of SBS1 and SBS2 remains to be fully understood. Mutational analysis of Tyr-380 situat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dcd8f4a4c0fda6e52c3c62d03462afa0
https://doi.org/10.1016/j.abb.2012.08.005
https://doi.org/10.1016/j.abb.2012.08.005
Autor:
Martin Willemoës, Birte Kramhøft, Birte Svensson, Samuel Tranier, Richard Haser, Sophie Bozonnet, Nushin Aghajari, Morten M. Nielsen, Morten T. Jensen, Malene H. Jensen
Publikováno v:
FEBS Journal. 274:5055-5067
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. This site on the non-ca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::86ba743daa93c4f50daf3c78ea48af18
https://doi.org/10.1111/j.1742-4658.2007.06024.x
https://doi.org/10.1111/j.1742-4658.2007.06024.x
Publikováno v:
FEBS Letters. 580:5049-5053
Subsite affinity maps of long substrate binding clefts in barley alpha-amylases, obtained using a series of maltooligosaccharides of degree of polymerization of 3-12, revealed unfavorable binding energies at the internal subsites -3 and -5 and at sub
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98fbce06a012f1657314a9edb81fda25
https://doi.org/10.1016/j.febslet.2006.08.028
https://doi.org/10.1016/j.febslet.2006.08.028
Autor:
Morten T. Jensen, X. Robert, Birgit Christine Bønsager, Nathalie Juge, Birte Svensson, S. Tranier, Richard Haser, Jane Nøhr, Martin Willemoës, M. Abou Hachem, Nushin Aghajari, Birte Kramhøft, Sophie Bozonnet, Kenji Fukuda
Publikováno v:
Biocatalysis and Biotransformation. 24:83-93
α-Amylases are endo-acting retaining enzymes of glycoside hydrolase family 13 with a catalytic (β/α)8-domain containing an inserted loop referred to as domain B and a C-terminal anti-parallel β-sheet termed domain C. New insights integrate the ro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f109cb46262e2492ca3c9d80e21fd0c5
https://doi.org/10.1080/10242420500516163
https://doi.org/10.1080/10242420500516163
Autor:
Kristian Sass Bak-Jensen, Nathalie Juge, Haruhide Mori, Jane Nøhr, Birte Kramhøft, Birte Svensson
Publikováno v:
Biochemistry. 44:1824-1832
Barley alpha-amylase 1 (AMY1) hydrolyzed amylose with a degree of multiple attack (DMA) of 1.9; that is, on average, 2.9 glycoside bonds are cleaved per productive enzyme-substrate encounter. Six AMY1 mutants, spanning the substrate binding cleft fro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aec7686d8a5f37cda9e0ff717532c429
https://doi.org/10.1021/bi048100v
https://doi.org/10.1021/bi048100v
Autor:
Birte Svensson, S. Bozonnet, T.-J. Kim, Peter Kresten Nielsen, Birgit C. Bønsager, Kristian Sass Bak-Jensen, Birte Kramhøft
Publikováno v:
Biocatalysis and Biotransformation. 21:209-214
Protein engineering of barley α-amylase addressed the roles of Ca2+ in activity and inhibition by barley α-amylase/subtilisin inhibitor (BASI), multiple attach in polysaccharide hydrolysis, secondary starch binding sites, and BASI hot spots in AMY2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a9ade7f9c38fade48111829e002481b
https://doi.org/10.1080/10242470310001618564
https://doi.org/10.1080/10242470310001618564
Autor:
Jane Nøhr, Christine Finnie, Nathalie Juge, Kristian Sass Bak-Jensen, Ole Østergaard, Birte Kramhøft, Birgit C. Bønsager, Peter Kresten Nielsen, Haruhide Mori, Birte Svensso
Publikováno v:
Journal of Applied Glycoscience. 50:277-282
Proteomes of barley seeds were described by 2-D gel electrophoresis and spots selected for proteinidentification by mass spectrometry and database searches. Proteins were categorised according to temporalappearance during seed development and maturat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a77760b990ccae56786282395b1be4d6
https://doi.org/10.5458/jag.50.277
https://doi.org/10.5458/jag.50.277
Autor:
Ole Olsen, Dedreia Tull, Søren Knudsen, Birte Svensson, Birte Kramhøft, Belinda A. Phillipson
Publikováno v:
Journal of Cereal Science. 37:71-80
Aleurone protoplasts were transfected to express synthetic genes encoding cytosolic and secreted forms of the alkalophilic Bacillus alpha -amylase, alkBA. The alpha -amylase activity in the cytosol of transfected protoplasts was increased 4 fold comp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::865daba398f3f63df309837f961dc2ee
https://doi.org/10.1006/jcrs.2002.0477
https://doi.org/10.1006/jcrs.2002.0477
Publikováno v:
Amino Acids. 13:281-297
Tetrahymena pyriformis suspended in an inorganic medium accumulates3H-labelled taurine against a concentration gradient resulting in a cellular to extracellular taurine gradient of about 3 within 2 hours. This is observed in spite of the fact that ta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b92d8d5a7c37dc2d347890bb37bc95e6
https://doi.org/10.1007/bf01372593
https://doi.org/10.1007/bf01372593
Publikováno v:
Cellular Physiology and Biochemistry. 3:97-110
HgCl2 (40 µM) initially activates an anion-independent unidirectional Na+ influx in Ehrlich ascites tumor cells, which amounts to 61 ± 7 µmol·g dry wt-1 min-1 (± SEM, n = 5). The unidirectional Na+ influx in control cells in 13 ± 2 µmol·dry w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1f7da59c88d0a7db4cfbf5da37bde95e
https://doi.org/10.1159/000154672
https://doi.org/10.1159/000154672