Výsledky vyhledávání - "Morten T. Jensen"

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

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

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Interactions of barley α-amylase isozymes with Ca2 + , substrates and proteinaceous inhibitors

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

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Differences in conformational stability of barley alpha-amylase isozymes 1 and 2. Role of charged groups and isozyme 2 specific salt-bridges

Autor: Tine E. Gottschalk, Birte Svensson, Morten T. Jensen

Publikováno v: Journal of Cereal Science. 38:289-300

Barley alpha-amylase isozymes 1 (AMY1) and 2 (AMY2) have 80% sequence identity but possess different physico-chemical properties. By incubation in the range 37–85 °C T50 is 75.2 °C of AMY1 and 79.2 °C of AMY2. While AMY2 is also most stable in u

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d62db728fa9375d105e5583d07fd8d4c
https://doi.org/10.1016/s0733-5210(03)00032-8

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Selection of a High-Energy Bioactive Conformation of a Sulfonium-Ion Glycosidase Inhibitor by the Enzyme Glucoamylase G2

Autor: Morten T. Jensen, B. Mario Pinto, Margaret A. Johnson, Birte Svensson

Publikováno v: Journal of the American Chemical Society. 125:5663-5670

Transferred nuclear Overhauser effect and rotating-frame Overhauser enhancement NMR spectroscopies are used to probe the conformation of a bicyclic sulfonium ion, which is an analogue of the naturally occurring glycosidase inhibitor castanospermine,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a5c804017d44c99c15bbe82634a8547
https://doi.org/10.1021/ja0212617

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Synthesis of Nitrogen Analogues of Salacinol and Their Evaluation as Glycosidase Inhibitors

Autor: Morten T. Jensen, Ahmad Ghavami, Birte Svensson, Blair D. Johnston, B. M. Pinto

Publikováno v: Technical University of Denmark Orbit

The syntheses of two nitrogen analogues (11 and 12) of the naturally occurring sulfonium ion, salacinol (7) are described. The latter compound is one of the active principles in the aqueous extracts of Salacia reticulata that are traditionally used i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f781393b1f91501ac536d756ef9c626
https://doi.org/10.1021/ja0103750

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