Zobrazeno 1 - 10 of 11 pro vyhledávání: '"Tine E, Gottschalk"'
1
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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2
The Structure of Barley α-Amylase Isozyme 1 Reveals a Novel Role of Domain C in Substrate Recognition and Binding
Autor: Fabien Ratajczak, Nushin Aghajari, Xavier Robert, Richard Haser, Tine E. Gottschalk, Birte Svensson, Hugues Driguez
Publikováno v: Structure. 11:973-984
Though the three-dimensional structures of barley alpha-amylase isozymes AMY1 and AMY2 are very similar, they differ remarkably from each other in their affinity for Ca(2+) and when interacting with substrate analogs. A surface site recognizing malto
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::efb0803dee6c344500461e932c3d3ee5
https://doi.org/10.1016/s0969-2126(03)00151-5
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3
Modulation of activity and substrate binding modes by mutation of single and double subsites +1/+2 and −5/−6 of barley α-amylase 1
Autor: Mohammed Saddik Motawia, Birger Lindberg Møller, Tine E. Gottschalk, Birte Svensson, Kristian Sass Bak-Jensen, Haruhide Mori, Iben Damager
Publikováno v: European Journal of Biochemistry. 268:6545-6558
Enzymatic properties of barley α-amylase 1 (AMY1) are altered as a result of amino acid substitutions at subsites −5/−6 (Cys95Ala/Thr) and +1/+2 (Met298Ala/Asn/Ser) as well as in the double mutants, Cys95Ala/Met298Ala/Asn/Ser. Cys95Ala shows 176
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::bc358a716ff22f611d426462d1d0e3c2
https://doi.org/10.1046/j.0014-2956.2001.02609.x
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4
Specificity Modulation of Barley α-Amylase through Biased Random Mutagenesis Involving a Conserved Tripeptide in β → α Loop 7 of the Catalytic (β/α)8-Barrel Domain
Autor: Tine E. Gottschalk, Dedreia Tull, Nushin Aghajari, Richard Haser, Birte Svensson
Publikováno v: Biochemistry. 40:12844-12854
The relative specificity and bond cleavage pattern of barley α-amylase 1 (AMY1) were dramatically changed by mutation in F286VD that connected β-strand 7 of the catalytic (β/α)8-barrel to a succeed...
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::39b49f29dba5056406d6372856d73f27
https://doi.org/10.1021/bi0108608
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5
Immunolocalization and characterization of a β-1,3-glucanase from sugar beet, deduction of its primary structure and nucleotide sequence by cDNA and genomic cloning
Autor: John E. Nielsen, Klaus K. Nielsen, Janne Brunstedt, Tine E. Gottschalk, Jørn Dalgaard Mikkelsen
Publikováno v: Plant Science. 132:153-167
A basic β -1,3-glucanase was found to accumulate in sugar beet ( Beta vulgaris ) leaves infected with the fungus Cercospora beticola . The subcellular distribution of the basic β -1,3-glucanase 2 in Cercospora infected sugar beets was studied by im
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b4f6607039ff292107f9faad2d393aba
https://doi.org/10.1016/s0168-9452(97)00255-0
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6
Tyrosine 105 and threonine 212 at outermost substrate binding subsites -6 and +4 control substrate specificity, oligosaccharide cleavage patterns, and multiple binding modes of barley alpha-amylase 1
Autor: Birte Svensson, Kristian Sass Bak-Jensen, Tine E. Gottschalk, Gabriel Paës, Vinh Tran, Gwenaelle André
Publikováno v: Journal of Biological Chemistry 11 (279), 10093-10102. (2004)
The role in activity of outer regions in the substrate binding cleft in alpha-amylases is illustrated by mutational analysis of Tyr(105) and Thr(212) localized at subsites -6 and +4 (substrate cleavage occurs between subsites -1 and +1) in barley alp
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc8af9297f60a7f8e65291405acfd4e7
https://pubmed.ncbi.nlm.nih.gov/14660599
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7
The structure of barley alpha-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding: a pair of sugar tongs
Autor: Xavier, Robert, Richard, Haser, Tine E, Gottschalk, Fabien, Ratajczak, Hugues, Driguez, Birte, Svensson, Nushin, Aghajari
Publikováno v: Structure (London, England : 1993). 11(8)
Though the three-dimensional structures of barley alpha-amylase isozymes AMY1 and AMY2 are very similar, they differ remarkably from each other in their affinity for Ca(2+) and when interacting with substrate analogs. A surface site recognizing malto
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::389b41bd722345fbb23a5cd3d942dac8
https://pubmed.ncbi.nlm.nih.gov/12906821
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8
Expression, purification and preliminary crystallographic studies of alpha-amylase isozyme 1 from barley seeds
Autor: Xavier Robert, Richard Haser, Tine E. Gottschalk, Birte Svensson, Nushin Aghajari
Publikováno v: Acta Crystallogr D Biol Crystallogr
Acta Crystallogr D Biol Crystallogr, 2002, 58, pp.683-686
Technical University of Denmark Orbit
HAL
International audience; The germinating barley seed contains two major alpha-amylase isozyme families, AMY1 and AMY2, involved in starch degradation to provide energy used by the plant embryo for growth. Many years of difficulty in growing three-dime
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::966e05d188cfd9be7b5682f92a88b346
https://hal.archives-ouvertes.fr/hal-00313546
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9
Extensive N-glycosylation reduces the thermal stability of a recombinant alkalophilic bacillus alpha-amylase produced in Pichia pastoris
Autor: Dedreia Tull, Birte Svensson, Birte Kramhøft, Henrik Bisgard-Frantzen, Ib Svendsen, Ole Olsen, Tine E. Gottschalk, Belinda A. Phillipson
Publikováno v: Protein expression and purification. 21(1)
Alkalophilic Bacillus alpha-amylase (ABA) was produced in the yeast Pichia pastoris with a yield of 50 mg L(-1) of culture supernatant. The recombinant protein, rABA, was glycosylated at seven of the nine sites for potential N-glycosylation as identi
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a57e323d8688d9a8090cd039ede10c6b
https://pubmed.ncbi.nlm.nih.gov/11162382
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