Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Tatsuya Ohshida"'
Publikováno v:
Frontiers in Microbiology, Vol 9 (2018)
We recently identified and characterized a novel broad substrate specificity amino acid racemase (BAR) from the hyperthermophilic archaeon Pyrococcus horikoshii OT-3. Three genes, PH0782, PH1423, and PH1501, encoding homologs exhibiting about 45% seq
Externí odkaz:
https://doaj.org/article/186dde9537bf4da798e518672390feda
Autor:
Tatsuya Ohshida, Kosaku Horinaga, Hiroaki Sakamoto, Tatsunari Hirano, Eiichiro Takamura, Takenori Satomura, Shin-ichiro Suye, Kohei Inagaki, Haruhiko Sakuraba, Toshihisa Ohshima
Publikováno v:
Journal of Biotechnology. 325:226-232
Although multicopper oxidase from the hyperthermophilic archaeon Pyrobaculum aerophilum (McoP) can be particularly useful in biotechnological applications, e.g., as a specific catalyst at the biocathode of biofuel cells (BFCs), owing to its high stab
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67b2cf01835134174fa34bc01699a28d
https://doi.org/10.1016/j.jbiotec.2020.10.019
https://doi.org/10.1016/j.jbiotec.2020.10.019
Autor:
Ryushi Kawakami, Tatsuya Ohshida, Junji Hayashi, Kazunari Yoneda, Toshio Furumoto, Toshihisa Ohshima, Haruhiko Sakuraba
Publikováno v:
International journal of biological macromolecules. 208
Ornithine δ-aminotransferase (Orn-AT) activity was detected for the enzyme annotated as a γ-aminobutyrate aminotransferase encoded by PH1423 gene from Pyrococcus horikoshii OT-3. Crystal structures of this novel archaeal ω-aminotransferase were de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f997ea536548a4fd47d5fa8294ade246
https://pubmed.ncbi.nlm.nih.gov/35337912
https://pubmed.ncbi.nlm.nih.gov/35337912
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 88:669-678
A gene encoding galactose 1-phosphate uridylyltransferase (GalT) was identified in the hyperthermophilic archaeon Pyrobaculum aerophilum. The gene was overexpressed in Escherichia coli, after which its product was purified and characterized. The expr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::940d8601ee68032153d8f85227c9c046
https://doi.org/10.1002/prot.25848
https://doi.org/10.1002/prot.25848
Autor:
Haruhiko Sakuraba, Toshihisa Ohshima, Kazunari Yoneda, Kohei Koba, Tatsuya Ohshida, Taketo Ohmori, Junji Hayashi
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 82:2084-2093
The orientation of the three domains in the bifunctional aspartate kinase-homoserine dehydrogenase (AK-HseDH) homologue found in Thermotoga maritima totally differs from those observed in previously known AK-HseDHs; the domains line up in the order H
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4c9c06fa9f09f0f981bd34a72a4ab26
https://doi.org/10.1080/09168451.2018.1511365
https://doi.org/10.1080/09168451.2018.1511365
Autor:
Toshihisa Ohshima, Takenori Satomura, Junji Hayashi, Shin-ichiro Suye, Haruhiko Sakuraba, Tatsuya Ohshida
Publikováno v:
Extremophiles. 22:975-981
A gene-encoding a dye-linked D-lactate dehydrogenase (Dye-DLDH) homolog was identified in the genome of the hyperthermophilic archaeon Thermoproteus tenax. The gene was expressed in Escherichia coli and the product was purified to homogeneity. The re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67e709f26a9a1d6b7a9bebcd97d6ec40
https://doi.org/10.1007/s00792-018-1054-3
https://doi.org/10.1007/s00792-018-1054-3
Autor:
Haruhiko Sakuraba, Tatsuya Ohshida, Takenori Satomura, Ryushi Kawakami, Toshihisa Ohshima, Junji Hayashi
Publikováno v:
Protein Expression and Purification. 126:62-68
2-Deoxy-d-ribose-5-phosphate aldolase (DERA) catalyzes the aldol reaction between two aldehydes and is thought to be a potential biocatalyst for the production of a variety of stereo-specific materials. A gene encoding DERA from the extreme halophili
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0aead3a0912e070487eb1a2e37e7b678
https://doi.org/10.1016/j.pep.2016.05.009
https://doi.org/10.1016/j.pep.2016.05.009
Publikováno v:
Frontiers in Microbiology, Vol 9 (2018)
We recently identified and characterized a novel broad substrate specificity amino acid racemase (BAR) from the hyperthermophilic archaeon Pyrococcus horikoshii OT-3. Three genes, PH0782, PH1423, and PH1501, encoding homologs exhibiting about 45% seq
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9d74871aeeeef5d331f5d445f3405f0
https://www.frontiersin.org/article/10.3389/fmicb.2018.01481/full
https://www.frontiersin.org/article/10.3389/fmicb.2018.01481/full