Výsledky vyhledávání - "Eiji Inagaki"

Expression, purification, crystallization and preliminary X-ray diffraction analysis of galactokinase fromPyrococcus horikoshii

Autor: Akeo Shinkai, Takaho Terada, Shigeyuki Yokoyama, Chizu Kuroishi, Eiji Inagaki, Keiko Sakamoto, Naomi Obayashi, Seiki Kuramitsu, Yoshitaka Bessho, Mikako Shirouzu

Publikováno v: Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62:169-171

Galactokinase (EC 2.7.1.6) catalyzes the ATP-dependent phosphorylation of alpha-D-galactose to alpha-D-galactose-1-phosphate, in an additional metabolic branch of glycolysis. The apo-form crystal structure of the enzyme has not yet been elucidated. C

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cddb685951f83799785afb6dcde028a4
https://doi.org/10.1107/s1744309106001813

Zobrazit plný text záznamu

Novel Renin Inhibitors Containing (2S,3S,5S)-2-Amino-1-cyclohexyl-6-methyl-3,5-heptanediol Fragment as a Transition-state Mimic at the P1-P1' Cleavage Site

Autor: Ikuro Nakamura, Yoshiharu Hayashi, Kiyoteru Ikegami, Itsuo Uchida, Eiji Shirakawa, Koji Ando, Hiroki Tada, Yasuki Yamada, Saizo Shibata, Eiji Inagaki, Yukishige Ikemoto

Publikováno v: Chemical and Pharmaceutical Bulletin. 45:1631-1641

A series of renin inhibitors containing the (2S,3S,5S)-2-amino-1-cyclohexyl-6-methyl-3,5-heptanediol (2-amino-3,5-anti-diol) fragment as a novel transition-state mimic was synthesized, and their biological activities were evaluated. All of the synthe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68dd26edbe61091598ec4d42ee83c36b
https://doi.org/10.1248/cpb.45.1631

Zobrazit plný text záznamu

X-ray Structure of a Pokeweed Antiviral Protein, Coded by a New Genomic Clone, at 0.23 nm Resolution. A Model Structure Provides a Suitable Electrostatic Field for Substrate Binding

Autor: Jiro Kataoka, Hideaki Tsuge, Eiji Inagaki, Noriyuki Habuka, Masashi Miyano, Hideo Ago, Masana Noma

Publikováno v: European Journal of Biochemistry. 225:369-374

We have determined the crystal structure of alpha-pokeweed antiviral protein, a member of ribosome-inactivating proteins, at 0.23 nm resolution, by the molecular-replacement method. The crystals belong to the space group P2(1)2(1)2 with unit-cell dim

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5faeda2f6c50d02732d4e7954c3744c2
https://doi.org/10.1111/j.1432-1033.1994.00369.x

Zobrazit plný text záznamu

The crystal and molecular structure of β-d-fructofuranosyl α-d-xylopyranoside hemihydrate

Autor: Eiji Inagaki, Tooru Taga, Kouki Fujita, Yoshihiro Fujimori, Kouzou Hara

Publikováno v: Carbohydrate Research. 241:63-69

The crystal and molecular structure of β- d -fructofuranosyl α- d -xylopyranoside (xylosucrose) hemihydrate, C 11 H 20 O 10 ·0.5H 2 O, is orthorhombic, P 2 1 2 1 2, with a = 20.919(5), b = 18.727(2), c = 7.071(1) A, V = 2770.1(2) A 3 , Z = 8, and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b3b16aaef487e8437a871f629a564a3
https://doi.org/10.1016/0008-6215(93)80095-v

Zobrazit plný text záznamu

New insights into the binding mode of coenzymes: structure of Thermus thermophilus Δ1-pyrroline-5-carboxylate dehydrogenase complexed with NADP+

Autor: Noriyasu Ohshima, Tahir H. Tahirov, Eiji Inagaki, Shigeyuki Yokoyama, Hiroaki Kato, Nigar D. Babayeva, Keiko Sakamoto

Delta(1)-Pyrroline-5-carboxylate dehydrogenase (P5CDh) is known to preferentially use NAD(+) as a coenzyme. The k(cat) value of Thermus thermophilus P5CDh (TtP5CDh) is four times lower for NADP(+) than for NAD(+). The crystal structure of NADP(+)-bou

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62a025d004284baeebbfa2821f2e939f
https://europepmc.org/articles/PMC2335078/

Zobrazit plný text záznamu

Crystal structure of Thermus thermophilus Delta1-pyrroline-5-carboxylate dehydrogenase

Autor: Eiji Inagaki, Shigeyuki Yokoyama, Noriyasu Ohshima, Hitomi Takahashi, Tahir H. Tahirov, Chizu Kuroishi

Publikováno v: Journal of molecular biology. 362(3)

Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDh) plays an important role in the metabolic pathway from proline to glutamate. It irreversibly catalyzes the oxidation of glutamate-gamma-semialdehyde, the product of the non-enzymatic hydrolysis of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74b9867fe47d8467722690666eb92549
https://pubmed.ncbi.nlm.nih.gov/16934832

Zobrazit plný text záznamu

Crystallization and avoiding the problem of hemihedral twinning in crystals of Delta1-pyrroline-5-carboxylate dehydrogenase from Thermus thermophilus

Autor: Chizu Kuroishi, Eiji Inagaki, Hitomi Takahashi, Tahir H. Tahirov

Publikováno v: Acta crystallographica. Section F, Structural biology and crystallization communications. 61(Pt 6)

Delta1-Pyrroline-5-carboxylate dehydrogenase from Thermus thermophilus (TtP5CDh) has been crystallized in a citrate-bound form (TtP5CDh-cit). The crystals diffracted to well beyond 2 A resolution, but exhibited perfect or near-perfect hemihedral twin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9eb3cea4b46bc45c1510173736ff917e
https://pubmed.ncbi.nlm.nih.gov/16511109

Zobrazit plný text záznamu

Structure of PIN-domain protein PH0500 from Pyrococcus horikoshii

Autor: Tahir H. Tahirov, Jeyaraman Jeyakanthan, Chizu Kuroishi, Eiji Inagaki

Publikováno v: Acta crystallographica. Section F, Structural biology and crystallization communications. 61(Pt 5)

The Pyrococcus horikoshii OT3 protein PH0500 is highly conserved within the Pyrococcus genus of hyperthermophilic archaea and shows low amino-acid sequence similarity with a family of PIN-domain proteins. The protein has been expressed, purified and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::109ac48e37572e0de24307bd11a5d0a4
https://pubmed.ncbi.nlm.nih.gov/16511069

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání