Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Taku, Ohki"'
Autor:
Seiji, Negoro, Dai-Ichiro, Kato, Taku, Ohki, Kengo, Yasuhira, Yasuyuki, Kawashima, Keisuke, Nagai, Masahiro, Takeo, Naoki, Shibata, Katsumasa, Kamiya, Yasuteru, Shigeta
Publikováno v:
Methods in enzymology. 648
Biodegradation of synthetic polymers is recognized as a useful way to reduce their environmental load and pollution, loss of natural resources, extensive energy consumption, and generation of greenhouse gases. The potential use of enzymes responsible
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4239ba33e4f354a6a432d2688aca7c4c
https://pubmed.ncbi.nlm.nih.gov/33579412
https://pubmed.ncbi.nlm.nih.gov/33579412
Autor:
Masahiro Takeo, Taku Ohki, Dai-ichiro Kato, Keisuke Nagai, Naoki Shibata, Katsumasa Kamiya, Yasuteru Shigeta, Kengo Yasuhira, Seiji Negoro, Yasuyuki Kawashima
Publikováno v:
Methods in Enzymology ISBN: 9780128220122
Biodegradation of synthetic polymers is recognized as a useful way to reduce their environmental load and pollution, loss of natural resources, extensive energy consumption, and generation of greenhouse gases. The potential use of enzymes responsible
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ff7e39629185142f0f4dd4850a2ec9f6
https://doi.org/10.1016/bs.mie.2020.11.004
https://doi.org/10.1016/bs.mie.2020.11.004
Autor:
Masahiro Takeo, Naoki Shibata, Dai-ichiro Kato, Taku Ohki, Yasuyuki Kawashima, Seiji Negoro, Yoshiki Higuchi
Publikováno v:
Protein Science. 18:1662-1673
Promiscuous 6-aminohexanoate-linear dimer (Ald)-hydrolytic activity originally obtained in a carboxylesterase with a beta-lactamase fold was enhanced about 80-fold by directed evolution using error-prone PCR and DNA shuffling. Kinetic studies of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a84e95eea74b429e4d7f07a86e26d1e
https://doi.org/10.1002/pro.185
https://doi.org/10.1002/pro.185
Autor:
Masahiro Takeo, Ichitaro Kawamoto, Keiji Matsumoto, Naoki Shibata, Junya Tsurukame, Yoshiki Higuchi, Seiji Negoro, Yoshiaki Wakitani, Nobuhiro Mizuno, Taku Ohki
Publikováno v:
Journal of Biological Chemistry. 280:39644-39652
6-Aminohexanoate-dimer hydrolase (EII), responsible for the degradation of nylon-6 industry by-products, and its analogous enzyme (EII′) that has only ∼0.5% of the specific activity toward the 6-aminohexanoate-linear dimer, are encoded on plasmid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::82a9f2666f4fd38eff0bbb300aa9f5ab
https://doi.org/10.1074/jbc.m505946200
https://doi.org/10.1074/jbc.m505946200
Autor:
Naoki Shibata, Yoshiki Higuchi, Yusuke Nakata, Dai-ichiro Kato, Taku Ohki, Seiji Negoro, Yasuyuki Kawashima, Masahiro Takeo, Yusuke Matsuura, Yoshiaki Wakitani
Publikováno v:
The FEBS journal. 276(9)
A carboxylesterase with a beta-lactamase fold from Arthrobacter possesses a low level of hydrolytic activity (0.023 mumol.min(-1).mg(-1)) when acting on a 6-aminohexanoate linear dimer byproduct of the nylon-6 industry (Ald). G181D/H266N/D370Y triple
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f824989f2f33e25515b5dc14476a9403
https://pubmed.ncbi.nlm.nih.gov/19476493
https://pubmed.ncbi.nlm.nih.gov/19476493
Autor:
Haruhisa Hayashi, Naoki Shibata, Kengo Yasuhira, Dai-ichiro Kato, Kazuhiro Sasa, Hidehiko Nakano, Masahiro Takeo, Yoshiki Higuchi, Taku Ohki, Seiji Negoro
Publikováno v:
Journal of molecular biology. 370(1)
We performed X-ray crystallographic analyses of 6-aminohexanoate-dimer hydrolase (Hyb-24DN), an enzyme responsible for the degradation of nylon-6, an industry by-product, and of a complex between Hyb-24DN-A(112) (S112A-mutant of Hyb-24DN) and 6-amino
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8d396e1de6394c7f8df3529ffc2813d
https://pubmed.ncbi.nlm.nih.gov/17512009
https://pubmed.ncbi.nlm.nih.gov/17512009
Autor:
Seiji Negoro, Taku Ohki, Yoshiki Higuchi, Naoki Shibata, Yoshiaki Wakitani, Kengo Yasuhira, Masahiro Takeo
Publikováno v:
FEBS letters. 580(21)
Carboxylesterase (EII′) from Arthrobacter sp. KI72 has 88% homology to 6-aminohexanoate-dimer hydrolase (EII) and possesses ca. 0.5% of the level of 6-aminohexanoate-linear dimer (Ald)-hydrolytic activity of EII. To study relationship between Ald-h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc5cb8700b48063cbbcc8531b0b69743
https://pubmed.ncbi.nlm.nih.gov/16949580
https://pubmed.ncbi.nlm.nih.gov/16949580
Autor:
Seiji, Negoro, Taku, Ohki, Naoki, Shibata, Nobuhiro, Mizuno, Yoshiaki, Wakitani, Junya, Tsurukame, Keiji, Matsumoto, Ichitaro, Kawamoto, Masahiro, Takeo, Yoshiki, Higuchi
Publikováno v:
The Journal of biological chemistry. 280(47)
6-Aminohexanoate-dimer hydrolase (EII), responsible for the degradation of nylon-6 industry by-products, and its analogous enzyme (EII') that has only approximately 0.5% of the specific activity toward the 6-aminohexanoate-linear dimer, are encoded o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f8ddc5057547967f08e1961f75e4c8cf
https://pubmed.ncbi.nlm.nih.gov/16162506
https://pubmed.ncbi.nlm.nih.gov/16162506
Publikováno v:
Acta crystallographica. Section F, Structural biology and crystallization communications. 61(Pt 10)
To investigate the structure-function relationship between 6-aminohexanoate-dimer hydrolase (EII) from Arthrobacter sp. and a cryptic protein (EII') which shows 88% sequence identity to EII, a hybrid protein (named Hyb-24) of EII and EII' was overexp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6791a3b79971a7077ad4cdaebe2fbd28
https://pubmed.ncbi.nlm.nih.gov/16511198
https://pubmed.ncbi.nlm.nih.gov/16511198
Publikováno v:
The Proceedings of Mechanical Engineering Congress, Japan. 2011:G150022-1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::33457991bc23dfa515cf695b5d6edd90
https://doi.org/10.1299/jsmemecj.2011._g150022-1
https://doi.org/10.1299/jsmemecj.2011._g150022-1