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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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Roles of multiple surface sites, long substrate binding clefts, and carbohydrate binding modules in the action of amylolytic enzymes on polysaccharide substrates

Autor: Birte Svensson, Lili Kandra, Henrik Næsted, Richard Haser, Sophie Bozonnet, Martin Willemoës, Morten M. Nielsen, M. Abou Hachem, Nushin Aghajari, Gyöngyi Gyémánt, Eun-Seong Seo, Adiphol Dilokpimol, Jimmy Andersen

Publikováno v: Nielsen, M M, Seo, E S, Dilokpimol, A, Andersen, J, Hachem, M A, Naested, H, Willemoës, M, Bozonnet, S, Kandra, L, Gyemant, G, Haser, R, Aghajari, N & Svensson, B 2008, ' Roles of multiple surface sites, long substrate binding clefts, and carbohydrate binding modules in the action of amylolytic enzymes on polysaccharide substrates ', Biocatalysis and Biotransformation, vol. 26, no. 1-2, pp. 59-67 . https://doi.org/10.1080/10242420701789528
Biocatalysis and Biotransformation
Biocatalysis and Biotransformation, Taylor & Francis, 2008, 26, pp.59-67
Technical University of Denmark Orbit
HAL

International audience; Germinating barley seeds contain multiple forms of alpha-amylase, which are subject to both differential gene expression and differential degradation as part of the repertoire of starch-degrading enzymes. The alpha-amylases ar

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21496a8673791eaf7dff5c0a137196ec
https://cris.vtt.fi/en/publications/d35b89a9-bbe7-432d-866d-be8d111a16bc