Zobrazeno 1 - 10
of 212
pro vyhledávání: '"Noritake Yasuoka"'
Autor:
Noritake Yasuoka
Publikováno v:
Nihon Kessho Gakkaishi. 62:200-200
Autor:
Naoki Shibata, Koichi Mori, Yoshiki Higuchi, Tetsuo Toraya, Hiroko Tamagaki, Naoki Hieda, Noritake Yasuoka, Hirofumi Komori, Shin Ichi Terawaki, Keita Akita, Yasuhito Shomura
Publikováno v:
Journal of Biological Chemistry. 285:26484-26493
N-terminal truncation of the Escherichia coli ethanolamine ammonia-lyase beta-subunit does not affect the catalytic properties of the enzyme (Akita, K., Hieda, N., Baba, N., Kawaguchi, S., Sakamoto, H., Nakanishi, Y., Yamanishi, M., Mori, K., and Tor
Autor:
Kyoko Suto, Hideo Inoue, Yoshiki Higuchi, Noritake Yasuoka, Masaya Kitamura, Takuto Hayashida, Koji Terakawa, Naoki Shibata, Yukio Morimoto
Publikováno v:
Journal of Biochemistry. 141:459-468
Mutants of flavin mononucleotide-binding protein (FMN-bp) were made by site-directed mutagenesis to investigate the role of carboxyl-terminal Leu122 of the pairing subunit in controlling redox potentials, binding the prosthetic group, and forming the
Autor:
Midori Sato, Kiyoshi Ozawa, Yukio Morimoto, Naoki Shibata, Yuki Takayama, Hideo Akutsu, Noritake Yasuoka, Yoshiki Higuchi
Publikováno v:
Journal of Synchrotron Radiation. 11:113-116
The crystal structures of high-molecular-weight cytochrome c (HMC) from Desulfovibrio vulgaris Hildenborough in the transient and reduced states have been determined at 2.8 A resolution. An absorption spectrum measured with microspectrophotometer ind
Publikováno v:
Biochemistry. 41:12607-12617
Substrate binding triggers catalytic radical formation through the cobalt-carbon bond homolysis in coenzyme B12-dependent enzymes. We have determined the crystal structure of the substrate-free form of Klebsiella oxytoca diol dehydratase*cyanocobalam
Autor:
Hideaki Sato, Mamoru Yamanishi, Naoki Shibata, Michio Yunoki, Junko Matsui, Kazunori Oe, Tetsuo Toraya, Ayako Dokiya, Yukio Morimoto, Noritake Yasuoka, Kyoko Suto, Yasuhiro Iuchi, Takamasa Tobimatsu
Publikováno v:
European Journal of Biochemistry. 269:4484-4494
Recombinant glycerol dehydratase of Klebsiella pneumoniae was purified to homogeneity. The subunit composition of the enzyme was most probably α2β2γ2. When (R)- and (S)-propane-1,2-diols were used independently as substrates, the rate with the (R)
Autor:
Keiji Tanaka, Noritake Yasuoka, Yukio Morimoto, Yoshikazu Tomisugi, Masaki Unno, Tomitake Tsukihara, Tsunehiro Mizushima
Publikováno v:
Structure. 10(5):609-618
The 20S proteasome is the catalytic portion of the 26S proteasome. Constitutively expressed mammalian 20S proteasomes have three active subunits, beta 1, beta 2, and beta 5, which are replaced in the immunoproteasome by interferon-gamma-inducible sub
Publikováno v:
Structure. 8(7):775-788
Background: Adenosylcobalamin (coenzyme B 12 ) serves as a cofactor for enzymatic radical reactions. The adenosyl radical, a catalytic radical in these reactions, is formed by homolysis of the cobalt–carbon bond of the coenzyme, although the mechan
Autor:
Akira Naito, Hiroki Akutsu, Yuya Ogawa, Noritake Yasuoka, Shin'ichi Nakatsuji, Jun-ichi Yamada, Soichi Takeuchi, Kyoko Sudo
Publikováno v:
Molecular Crystals and Liquid Crystals Science and Technology. Section A. Molecular Crystals and Liquid Crystals. 345:167-172
A couple of spin systems with photo-responsive property have been developed, i. e., norbor-nadiene and spiropyran derivatives carrying TEMPO-substituent and their light-induced structural changes to the corresponding quadricyclane or merocyanine deri
Autor:
Naoki Shibata, Tomitake Tsukihara, Noritake Yasuoka, Yukdo Morimoto, Takashi Kinebuchi, Takashi Matsumoto, Nobuo Shimamoto
Publikováno v:
Journal of Biochemistry. 127:329-335
The single-stranded DNA (ssDNA) binding protein from Escherichia coli (EcoSSB) plays a central role in DNA replication, recombination and repair. The tertiary structure of EcoSSB was determined at 2.2 A resolution. This is rather higher resolution th