Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Hirokazu Nanba"'
Autor:
Junzo Hasegawa, Ryota Yanai, Daisuke Moriyama, Motohisa Washida, Makoto Kawamukai, Tomohiro Kaino, Hirokazu Nanba, Yasuhiro Ikenaka, Kazuyoshi Yajima
Publikováno v:
Applied genetics and molecular biotechnology. 101(4):1559-1571
Coenzyme Q (CoQ) is composed of a benzoquinone moiety and an isoprenoid side chain of varying lengths. The length of the side chain is controlled by polyprenyl diphosphate synthase. In this study, dps1 genes encoding decaprenyl diphosphate synthase w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c3fccd401d43f52eb07ec98bb1a1243
http://ir.lib.shimane-u.ac.jp/49381
http://ir.lib.shimane-u.ac.jp/49381
Autor:
Makoto Kawamukai, Makoto Fujii, Daisuke Moriyama, Hirokazu Nanba, Tomohiro Kaino, Motohisa Washida, Kouji Hosono
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 79:1026-1033
Coenzyme Q10 (CoQ10) is essential for energy production and has become a popular supplement in recent years. In this study, CoQ10 productivity was improved in the fission yeast Schizosaccharomyces pombe. Ten CoQ biosynthetic genes were cloned and ove
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41f598346b1ae1cd3743e8debd0a1d73
https://doi.org/10.1080/09168451.2015.1006573
https://doi.org/10.1080/09168451.2015.1006573
Autor:
Satohiro Yanagisawa, Hirokazu Nanba, Kohei Mori, Makoto Ueda, Masanobu Sugawara, Nobuo Nagashima, Kenji Inoue, Takahiro Ohishi, Tatsuya Honda, Masashi Izumida
Publikováno v:
Tetrahedron Letters. 48:3437-3440
A scalable and cost-effective synthesis of d - and l -α-methylcysteine is described. A key step is d -selective cyclization of N-carbamoyl S-tert-butyl- d , l -α-methylcysteine catalyzed by hydantoinase. d -5-tert-Butylthiomethyl-5-methylhydantoin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7b8d9422c521f65eaf8eb04ce400c0ed
https://doi.org/10.1016/j.tetlet.2007.03.040
https://doi.org/10.1016/j.tetlet.2007.03.040
Autor:
Hirokazu Nanba, Junzo Hasegawa, Takahisa Nakai, Yoshihiko Yasohara, Souichi Morikawa, Noriyuki Kizaki
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 69:544-552
A wild type NADPH-dependent carbonyl reductase from Candida magnoliae (reductase S1) has been found not to utilize NADH as a coenzyme. A mutation to exchange the coenzyme specificity in reductase S1 has been designed by computer-aided methods, includ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3582d863401f25e679264126c020c1b8
https://doi.org/10.1271/bbb.69.544
https://doi.org/10.1271/bbb.69.544
Publikováno v:
Journal of the agricultural chemical society of Japan. 74:961-966
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::700cd54e4cde741e64aa92e234a32b8b
https://doi.org/10.1271/nogeikagaku1924.74.961
https://doi.org/10.1271/nogeikagaku1924.74.961
Autor:
Sheng-Xue Xie, Satomi Takahashi, Yasuhiro Ikenaka, R. M. Vohra, Jun Ogawa, R. Indrati, H. Miyakawa, Tamio Ueno, Sakayu Shimizu, Atsushi Ryono, Hirokazu Nanba
Publikováno v:
Applied Microbiology and Biotechnology. 52:797-801
N-Carbamoyl-d-α-amino acid amidohydrolase (d-carbamoylase) was found to distinguish stereochemistry not only at the α-carbon but also at the β-carbon of N-carbamoyl-d-α-amino acids. The enzyme selectively acted on one of the four stereoisomers of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8168af9c4f40d8bdcbed9134265f0156
https://doi.org/10.1007/s002530051594
https://doi.org/10.1007/s002530051594
Autor:
Masayuki Takano, Kazuhiko Yamada, Yukio Yamada, Satomi Takahashi, Kazuma Ohkubo, Kazuyoshi Yajima, Hirokazu Nanba, Yoshirou Hiraishi, Yasuhiro Ikenaka
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 6:257-263
N-Carbamyl- d -amino acid amidohydrolase (DCase), in which amino acid residues were substituted by mutation, followed by the selection based on thermotolerance, showed improved thermostability, by 5° or 10°C, compared to the native DCase. These DCa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a3bc30f2e7a85fd8cf0abdb0ddd89484
https://doi.org/10.1016/s1381-1177(98)00078-2
https://doi.org/10.1016/s1381-1177(98)00078-2
Autor:
Satomi Takahashi, Yukio Yamada, Yasuhiro Ikenaka, Hirokazu Nanba, Masayuki Takano, Kazuyoshi Yajima
Publikováno v:
Journal of Bioscience and Bioengineering. 87:149-154
A plasmid, pNT4553, was constructed for high level production of N-carbamyl-d-amino acid amidohydrolase (DCase), the thermostability of which has been improved by amino acid substitution. The DCase activity and the stability of the plasmid in the hos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed80a6575c6bc7f4f87bed8dd74950e0
https://doi.org/10.1016/s1389-1723(99)89004-5
https://doi.org/10.1016/s1389-1723(99)89004-5
Autor:
Yukio Yamada, Satomi Takahashi, Yasuhiro Ikenaka, Hirokazu Nanba, Masayuki Takano, Kazuyoshi Yajima
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 62:1672-1675
For the production of D-amino acids using stable N-carbamyl-D-amino acid amidohydrolase (DCase) in an immobilized form, the DCase gene of Agrobacterium sp. KNK712 was mutagenized to increase its enzymatic thermostability. In a search for thermostabil
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e79b56485560afd2021ef863d08ce170
https://doi.org/10.1271/bbb.62.1672
https://doi.org/10.1271/bbb.62.1672
Autor:
Yasuhiro Ikenaka, Masayuki Takano, Kazuyoshi Yajima, Hirokazu Nanba, Satomi Takahashi, Yukio Yamada
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 62:1668-1671
To improve the production of D-amino acids using an immobilized N-carbamyl-D-amino acid amidohydrolase, the enzyme gene of Agrobacterium sp. KNK712 was mutagenized randomly to increase its thermostability. The gene was inserted into M13mp19, mutageni
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::287c7b07a6d11bf55e1ab0440c0f15dd
https://doi.org/10.1271/bbb.62.1668
https://doi.org/10.1271/bbb.62.1668