Zobrazeno 1 - 10
of 329
pro vyhledávání: '"Taka-Amylase A"'
Akademický článek
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Publikováno v:
Mycologia, 1998 Jul 01. 90(4), 618-623.
Externí odkaz:
https://www.jstor.org/stable/3761221
Akademický článek
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Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
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Autor:
A. Vujicic-Zagar, B.W. Dijkstra
Publikováno v:
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 62, 716-721
Aspergillus niger alpha-amylase catalyses the hydrolysis of alpha-1,4-glucosidic bonds in starch. It shows 100% sequence identity to the A. oryzae homologue (also called TAKA-amylase), three crystal structures of which have been published to date. Tw
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46c10e2a08ac7b807aa0841d932d7b07
https://hdl.handle.net/11370/58fb2fe3-8d6d-40f9-84ff-88f44384a928
https://hdl.handle.net/11370/58fb2fe3-8d6d-40f9-84ff-88f44384a928
Autor:
Jaap Visser, Satoshi Mimura, Leo H. de Graaff, Masashi Kato, Akimitsu Tanaka, Noriyuki Kitamoto, Norihiro Tsukagoshi, Junichiro Marui, Tetsuo Kobayashi
Publikováno v:
Fungal Genetics and Biology, 35(2), 157-169
Fungal Genetics and Biology 35 (2002) 2
Fungal Genetics and Biology 35 (2002) 2
By deletion across the promoter region of the xynF1 gene encoding the major Aspergillus oryzae xylanase, a 53-bp DNA fragment containing the XlnR binding sequence GGCTAAA as well as two similar sequences was shown to confer xylan inducibility on the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::490a9fb2aaf6015bdf1daa74dd51518d
https://doi.org/10.1006/fgbi.2001.1321
https://doi.org/10.1006/fgbi.2001.1321
Publikováno v:
Journal of Applied Glycoscience. 46:449-452
The modification of amino groups in Taka-amylase A (TAA) using trinitrobenzene sulfonic acid (TNBS), formaldehyde, and pyridoxal 5'-phosphate (PLP) was compared with that using a fluorescent reagent, ο-phthalaldehyde (OPA). Although OPA resulted in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2b363557a30a546844df428e62d120c6
https://doi.org/10.5458/jag.46.449
https://doi.org/10.5458/jag.46.449
Publikováno v:
Journal of Applied Glycoscience. 46:407-412
Cross-linked modifications of Taka-amylase A (TAA) with various dialdehyde derivatives including starch- and dextran-dialdehyde were examined. A rapid and significant decrease in the amount of free amino groups and enzyme activity of TAA was attained
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d1ba31ee27c6d460280036d33ac47e2d
https://doi.org/10.5458/jag.46.407
https://doi.org/10.5458/jag.46.407
Autor:
Bauke W. Dijkstra, Onno G. Faber, Henriëtte J. Rozeboom, D. Penninga, Lubbert Dijkhuizen, Boris Strokopytov, Ronald M.A. Knegtel, Kor H. Kalk
Publikováno v:
The Journal of Biological Chemistry, 270(49), 29256-29264. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Asp-229, Glu-257, and Asp-328 constitute the catalytic residues in cyclodextrin glycosyl transferase from Bacillus circulans strain 251. Via site-directed mutagenesis constructed D229N, E257Q, and D328N mutant proteins showed a 4,000-60,000 fold redu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5e143c87502362e441740c6be6d9da9
https://doi.org/10.1074/jbc.270.49.29256
https://doi.org/10.1074/jbc.270.49.29256
Autor:
Mikihiko Kobayashi, Setsuko Ohya
Publikováno v:
Carbohydrate Research. 237:263-270
Cyclomalto-oligosaccharides ( α-, β -, and γ -cyclodextrins) were partially oxidized by sodium meta-periodate, yielding the dialdehyde forms (D-CDs). Reduction of the D-CDs by sodium borohydride gave the corresponding alcohols (D-CD/Rs). Column ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::74c47789095a2414093df3b5f076e553
https://doi.org/10.1016/s0008-6215(92)84248-q
https://doi.org/10.1016/s0008-6215(92)84248-q