Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Hayuki Sugimoto"'
Autor:
Takeshi Watanabe, Dinh Minh Tran, Mizuki Shima, Iuliia Pentekhina, Tatsuyuki Hattori, Hayuki Sugimoto, Kazushi Suzuki
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 84:1936-1947
The genes encoding chitin-degrading enzymes in Aeromonas salmonicida SWSY-1.411 were identified and cloned in Escherichia coli. The strain contained two glycoside hydrolase (GH) families 18 chitinases: AsChiA and AsChiB, two GH19 chitinases: AsChiC a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::87aada01ea09c730487914e2d99d94b0
https://doi.org/10.1080/09168451.2020.1771539
https://doi.org/10.1080/09168451.2020.1771539
Autor:
Iuliia, Pentekhina, Tatsuyuki, Hattori, Dinh Minh, Tran, Mizuki, Shima, Takeshi, Watanabe, Hayuki, Sugimoto, Kazushi, Suzuki
Publikováno v:
Bioscience, biotechnology, and biochemistry. 84(9)
The genes encoding chitin-degrading enzymes in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b758d35db3c575ad2d5f30d65b1b7650
https://pubmed.ncbi.nlm.nih.gov/32471324
https://pubmed.ncbi.nlm.nih.gov/32471324
Autor:
Iuliia Pentekhina, Hattori, Tatsuyuki, Tran, Dinh Minh, Shima, Mizuki, Watanabe, Takeshi, Hayuki Sugimoto, Suzuki, Kazushi
The genes encoding chitin-degrading enzymes in Aeromonas salmonicida SWSY-1.411 were identified and cloned in Escherichia coli. The strain contained two glycoside hydrolase (GH) families 18 chitinases: AsChiA and AsChiB, two GH19 chitinases: AsChiC a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::131a002ff159b81eb2839e4cb4545302
Autor:
Takahisa Ikegami, Takeshi Watanabe, Hiroki Tanaka, Hayuki Sugimoto, Masashi Hara, Hideo Akutsu, Toshimichi Fujiwara, Izumi Yabuta
Publikováno v:
FEBS Letters. 592:3173-3182
Chitin-binding domain of chitinase A1 (ChBDChiA1 ) is characteristic because it binds only to insoluble crystalline chitin. While binding sites of major carbohydrate-binding modules carry multiple aromatic rings aligned on a surface, lethal mutations
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c4594d780639a5a8b8607c1e7aa71e8
https://doi.org/10.1002/1873-3468.13226
https://doi.org/10.1002/1873-3468.13226
Autor:
Toshiya Kozai, Kazushi Suzuki, Mayu Hara, Hiroyuki Noji, Tomoyuki Tasaki, Akihiko Nakamura, Ryota Iino, Takeshi Watanabe, Chihong Song, Kazuyoshi Murata, Yasuko Okuni, Hayuki Sugimoto, Takayuki Uchihashi
Publikováno v:
Physical Chemistry Chemical Physics. 20:3010-3018
Serratia marcescens chitinase A is a linear molecular motor that hydrolyses crystalline chitin in a processive manner. Here, we quantitatively determined the rate constants of elementary reaction steps, including binding (kon), translational movement
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2ebd2b89a739fa181067b6e1d3da742
https://doi.org/10.1039/c7cp04606e
https://doi.org/10.1039/c7cp04606e
Autor:
Akihiko Nakamura, Tomoyuki Tasaki, Yasuko Okuni, Chihong Song, Kazuyoshi Murata, Toshiya Kozai, Mayu Hara, Hayuki Sugimoto, Kazushi Suzuki, Takeshi Watanabe, Takayuki Uchihashi, Hiroyuki Noji, Ryota Iino
Publikováno v:
Physical chemistry chemical physics : PCCP. 20(5)
Correction for ‘Rate constants, processivity, and productive binding ratio of chitinase A revealed by single-molecule analysis’ by Akihiko Nakamura et al., Phys. Chem. Chem. Phys., 2018, DOI: 10.1039/c7cp04606e.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19f88fa57ec5b099d4a54817577aef84
https://pubmed.ncbi.nlm.nih.gov/29090301
https://pubmed.ncbi.nlm.nih.gov/29090301
To develop a novel type of biocontrol agent, we focus on bacteria that are characterized by both chitinase activity and biofilm development. Chitinolytic bacteria were isolated from sediments and chitin flakes immersed in the water of a sand dune lak
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fdf74421080ee2e566b81a724979ac4c
Autor:
Takeshi Watanabe, Takahisa Ikegami, Ken-ichi Akagi, Kazushi Suzuki, Masashi Hara, Michio Uemura, Hayuki Sugimoto
Publikováno v:
Journal of Biochemistry. 154:185-193
Chitinase A1 (ChiA1) from Bacillus circulans WL-12 comprises an N-terminal catalytic domain, two fibronectin type III domains, and a C-terminal chitin-binding domain (ChBD). The ChBD of ChiA1 (ChBDChiA1) belongs to carbohydrate-binding module (CBM) f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::414c5016cd765335a31f1f68501f40d6
https://doi.org/10.1093/jb/mvt043
https://doi.org/10.1093/jb/mvt043
Autor:
Akiko Fujinuma, Takeshi Watanabe, Yuji Nishino, Yuta Idezawa, Hayuki Sugimoto, Keita Nakamura, Kazushi Suzuki
Publikováno v:
The Journal of general and applied microbiology. 61(6)
Chitinase B from Serratia marcescens 2170 is one of the processive chitinases, and it has a linear path of aromatic amino acid residues on the surface and in the catalytic cleft. There are four surface-exposed residues lined-up towards the cleft, Y48
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23d7f49c80d1879a044b69cb17a14b63
https://pubmed.ncbi.nlm.nih.gov/26782656
https://pubmed.ncbi.nlm.nih.gov/26782656
Regulation of Chitinase Production by the 5'-Untranslated Region of theybfMinSerratia marcescens2170
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 76:1920-1924
Serratia marcescens 2170 produces three chitinases and the chitin-binding protein CBP21, and efficiently degrades insoluble and crystalline chitin. The three chitinases and CBP21 are induced by N,N'-diacetylchitobiose [(GlcNAc)₂], the major product
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd4c71cda6e4f6cee75214a2844debc1
https://doi.org/10.1271/bbb.120403
https://doi.org/10.1271/bbb.120403