Zobrazeno 1 - 10
of 58
pro vyhledávání: '"Takao, Torikata"'
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 79:196-204
To characterize the hydrogen-bonding network in lysozyme, we focused on the residue of Asp48 located at the active site in hen egg-white lysozyme. We constructed a mutant lysozyme (D48A) and analyzed using (GlcNAc)3 and chitin-affinity chromatography
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21f20517e7f80c5e9dfd64d7da843586
https://doi.org/10.1080/09168451.2014.963502
https://doi.org/10.1080/09168451.2014.963502
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 76:691-698
The amino acid sequence of Egyptian goose lysozyme (EGL) from egg-white and its enzymatic properties were analyzed. The established sequence had the highest similarity to wood duck lysozyme (WDL) with five amino acid substitutions, and had eighteen s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05ffdd22ea3e2588fd84cc2a54c503b0
https://doi.org/10.1271/bbb.110819
https://doi.org/10.1271/bbb.110819
Autor:
Satoru Kuhara, Hideki Hirakawa, Yoshihiro Kawahara, Shunsuke Kawamura, Atsuko Ochi, Takao Torikata
Publikováno v:
Journal of Biochemistry. 144:753-761
Despite the low similarity between their amino acid sequences, the core structures of the fold between chicken-type and goose-type lysozymes are conserved. However, their enzymatic activities are quite different. Both of them exhibit hydrolytic activ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b815959048a070e96a0b89ece24b5f2
https://doi.org/10.1093/jb/mvn133
https://doi.org/10.1093/jb/mvn133
Autor:
Takao Torikata, Satoru Kuhara, Hideki Hirakawa, Shunsuke Kawamura, Yuki Chijiiwa, Mari Ohkuma, Hiroyuki Nakagawa, Daiki Kohno
Publikováno v:
FEBS Journal. 275:2818-2830
The role of the two disulfide bonds (Cys4–Cys60 and Cys18–Cys29) in the activity and stability of goose-type (G-type) lysozyme was investigated using ostrich egg-white lysozyme as a model. Each of the two disulfide bonds was deleted separately or
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ec8cfa6486e5fedbf62d8def1fa6a7c2
https://doi.org/10.1111/j.1742-4658.2008.06422.x
https://doi.org/10.1111/j.1742-4658.2008.06422.x
Autor:
Toshie Minematsu, Yuki Chijiiwa, Shunsuke Kawamura, Takao Torikata, Kjell M. Vårum, Tamo Fukamizo
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 72:823-832
To understand better the role of subsites E and F in lysozyme-catalyzed reactions, mutant enzymes, in which Arg114, located on the right side of subsites E and F in hen egg-white lysozyme (HEL), was replaced with Lys, His, or Ala, were prepared. Repl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::171baaca64e6fd9286b08d90b61ccde0
https://doi.org/10.1271/bbb.70694
https://doi.org/10.1271/bbb.70694
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 68:159-169
G-type lysozyme is a hydrolytic enzyme sharing a similar tertiary structure with plant chitinase. To discover the relation of function and structure, we analyzed the primary structure of new G-type lysozyme. The complete 185 amino acid residues of ly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5338fa7d4218caa97aee3addfc3f3ec1
https://doi.org/10.1271/bbb.68.159
https://doi.org/10.1271/bbb.68.159
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 67:2621-2626
The amino acid sequence of satyr tragopan lysozyme and its activity was analyzed. Carboxymethylated lysozyme was digested with trypsin and the resulting peptides were sequenced. The established amino acid sequence had three amino acid substitutions a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2d4186f252585577e5302cb89097a3e
https://doi.org/10.1271/bbb.67.2621
https://doi.org/10.1271/bbb.67.2621
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 67:540-546
The courses of the reaction catalyzed by guinea hen egg-white lysozyme (GHL), in which Asn113 and Arg114 at subsites E and F in hen egg-white lysozyme (HEL) are replaced by Lys and His, respectively, was studied with the substrate N-acetylglucosamine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a3b1bdd1f7e52c1ca25eec648dd43e1
https://doi.org/10.1271/bbb.67.540
https://doi.org/10.1271/bbb.67.540
Publikováno v:
Journal of Biochemistry. 131:663-670
We analyzed the enzymatic properties of duck egg-white lysozyme II (DEL), which differs from hen egg-white lysozyme (HEL) in nineteen amino acid substitutions. A substrate binding study showed that DEL binds to the substrate analog at subsites A-C in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb6f7873eef76f5c75d444e00be22426
https://doi.org/10.1093/oxfordjournals.jbchem.a003149
https://doi.org/10.1093/oxfordjournals.jbchem.a003149
Autor:
Tamo Fukamizo, Tsugihisa Yamaguchi, Are Kristiansen, Takao Torikata, Kjell M. Vårum, Tomohiro Araki
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 65:1766-1773
Binding of a highly de-N-acetylated chitosan to Japanese pheasant lysozyme (JPL), which differs from hen egg white lysozyme (HEWL) by nine amino acid substitutions (including Arg114-->His), was investigated by 1H-NMR spectroscopy. The profile of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f79496abae5da4c34a257f804d07c363
https://doi.org/10.1271/bbb.65.1766
https://doi.org/10.1271/bbb.65.1766