Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Misumi Kataoka"'
Publikováno v:
Carbohydrate research. 522
Glycoside hydrolase family 12 endocellulase (GH family12) plays a key role in the degradation of β-glucan and cellulose. Hyperthermostable GH family 12 endocellulase from the archaeon Pyrococcus furiosus (EGPf) catalyzes the hydrolysis of β(1 → 4
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebe88ab407acdc257f855674211fd45b
https://pubmed.ncbi.nlm.nih.gov/36194965
https://pubmed.ncbi.nlm.nih.gov/36194965
Autor:
Akio Hamaguchi, Shota Nakanishi, Toshihide Okajima, Misumi Kataoka, Yoshiaki Kawano, Tadashi Nakai, Takeshi Murakawa, Katsuyuki Tanizawa, Hiroshi Yamaguchi, Hideyuki Hayashi
Publikováno v:
Journal of Biological Chemistry. 290:23094-23109
The catalytic reaction of copper amine oxidase proceeds through a ping-pong mechanism comprising two half-reactions. In the initial half-reaction, the substrate amine reduces the Tyr-derived cofactor, topa quinone (TPQ), to an aminoresorcinol form (T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f8203be667509b89a907a9d8af2b11d
https://doi.org/10.1074/jbc.m115.662726
https://doi.org/10.1074/jbc.m115.662726
Autor:
Shotaro Yamaguchi, Toshiaki Yanamoto, Satoru Ishihara, Makoto Nakabayashi, Kazuhiko Ishikawa, Misumi Kataoka, Masahiro Watanabe
Publikováno v:
FEBS Journal. 282:2540-2552
UNLABELLED β-Galactosidase (EC 3.2.1.23) from Bacillus circulans ATCC 31382, designated BgaD, exhibits high transglycosylation activity to produce galacto-oligosaccharides. BgaD has been speculated to have a multiple domain architecture including a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df14843cc91d20c704cbff6e59451aec
https://doi.org/10.1111/febs.13298
https://doi.org/10.1111/febs.13298
Publikováno v:
Acta Crystallographica. Section F, Structural Biology Communications
A protein-engineering study revealed that the C-terminal domain of a thermostable β-glucosidase contributes to its polymeric state.
One of the β-glucosidases from Pyrococcus furiosus (BGLPf) is found to be a hyperthermophilic tetrameric enzyme
One of the β-glucosidases from Pyrococcus furiosus (BGLPf) is found to be a hyperthermophilic tetrameric enzyme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5cb3bdc25a7b840746784904fe00c174
http://europepmc.org/articles/PMC4089520
http://europepmc.org/articles/PMC4089520
Publikováno v:
Acta Crystallographica Section D: Biological Crystallography
Substitutive mutations that convert a tetrameric β-glucosidase into a dimeric state lead to improvement of its crystal quality.
β-Glucosidase from Pyrococcus furiosus (BGLPf) is a hyperthermophilic tetrameric enzyme which can degrade celloolig
β-Glucosidase from Pyrococcus furiosus (BGLPf) is a hyperthermophilic tetrameric enzyme which can degrade celloolig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3c140b4f4c49d799f416c02a2d81c0b
https://doi.org/10.1107/s1399004713032276
https://doi.org/10.1107/s1399004713032276
Autor:
Kohei Kunimoto, Emi Takeda, Takashi Nakamura, Kazuhiko Ishikawa, Yoshito Kawai, Misumi Kataoka
Publikováno v:
Extremophiles : life under extreme conditions. 20(5)
O-Phosphoserine sulfhydrylase (OPSS) synthesizes cysteine from O-phospho-L-serine (OPS) and sulfide. We have determined the three-dimensional structures of OPSS from hyperthermophilic archaeon Aeropyrum pernix K1 (ApOPSS) in complex with aminoacrylat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4857554dd4f3cd6e8375fafa3d70129
https://pubmed.ncbi.nlm.nih.gov/27377295
https://pubmed.ncbi.nlm.nih.gov/27377295
Autor:
Hiroshi Yamaguchi, Toshihide Okajima, Ayuko Tominaga, Katsuyuki Tanizawa, Misumi Kataoka, Masayuki Otsu, Hiroko Oya
Publikováno v:
Journal of Synchrotron Radiation
Consecutive temporal analyses of enzyme structure have been performed during reactions in order to clarify the structure-based reaction mechanism. Four intermediate structures have been determined.
To reveal the chemical changes and geometry cha
To reveal the chemical changes and geometry cha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::761645e6191a406aad2fbcbb2dbdca64
https://doi.org/10.1107/s0909049510034989
https://doi.org/10.1107/s0909049510034989
Autor:
Misumi Kataoka, Akio Kumagai, Seiichiro Kishishita, Kazuhiko Ishikawa, Tatsuya Fujii, Hiroyuki Inoue
Publikováno v:
Biotechnology for Biofuels
Background Enzymatic removal of hemicellulose components such as xylan is an important factor for maintaining high glucose conversion from lignocelluloses subjected to low-severity pretreatment. Supplementation of xylanase in the cellulase mixture en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0e57be9be58de8dfcf28c329aadef90
https://doi.org/10.1186/s13068-015-0259-2
https://doi.org/10.1186/s13068-015-0259-2
Autor:
Misumi Kataoka, Kazuhiko Ishikawa
Publikováno v:
Bioscience, biotechnology, and biochemistry. 78(9)
Hyperthermophilic cellulase is an industrially important enzyme for biomass saccharification at high temperature. Two hyperthermophilic cellulases from the hyperthermophile Pyrococcus furiosus, endocellulase (EGPf) and β-glucosidase (BGLPf), exhibit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eefd7be652d2c5a161e6cddfa8849a1d
https://pubmed.ncbi.nlm.nih.gov/25209501
https://pubmed.ncbi.nlm.nih.gov/25209501
Autor:
Misumi Kataoka, Kazuhiko Ishikawa, Yoshito Kawai, Yuka Iwasaki, Takashi Nakamura, Kohei Kunimoto, Kaoru Nishii
Publikováno v:
Journal of molecular biology. 422(1)
l-Cysteine is synthesized from O-acetyl-l-serine (OAS) and sulfide by O-acetylserine sulfhydrylase (OASS; EC 2.5.1.47) in plants and bacteria. O-phosphoserine sulfhydrylase (OPSS; EC 2.5.1.65) is a novel enzyme from the hyperthermophilic aerobic arch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc86ef2899182c536423bccdff8b84d7
https://pubmed.ncbi.nlm.nih.gov/22580223
https://pubmed.ncbi.nlm.nih.gov/22580223