Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Gen Ichi Sampei"'
Publikováno v:
Acta Crystallogr F Struct Biol Commun
The thymidylate synthases ThyA and Thy1 are enzymes that catalyse the formation of thymidine monophosphate from 2′-deoxyuridine monophosphate. Thy1 (or ThyX) requires flavin for catalytic reactions, while ThyA does not. In the present study, the cr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9782215f4ecca5c0a53951d56a25d829
https://doi.org/10.1107/s2053230x19007192
https://doi.org/10.1107/s2053230x19007192
Publikováno v:
Journal of biochemistry. 168(3)
The crystal structure of an adenylate kinase from an extremophilic archaeon Aeropyrum pernix was determined in complex with full ligands, ATP-Mg2+ and AMP, at a resolution of 2.0 Å. The protein forms a trimer as found for other adenylate kinases fro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60da9a1dee531ad25a5409e8fa1f0b72
https://pubmed.ncbi.nlm.nih.gov/32271910
https://pubmed.ncbi.nlm.nih.gov/32271910
Publikováno v:
The Journal of Biochemistry. 162:423-430
By using the data obtained by the DNA microarray analysis for the intergenic regions applied to RNA samples extracted from Thermus thermophilus HB8, seven small non-coding RNAs, TtR-1 to TtR-7, were found to be expressed in the cells growing in rich
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d6c9e2e9e3b5fde01540eb3475bc708
https://doi.org/10.1093/jb/mvx046
https://doi.org/10.1093/jb/mvx046
Autor:
Lirong Chen, Yuzo Watanabe, Gota Kawai, Bi-Cheng Wang, Zheng-Qing Fu, Akio Ebihara, Sakiko Suzuki, Hisaaki Yanai, Ryoji Masui, Satoko Tamura, Kiyoshi Okada, Seiki Kuramitsu, Shigeyuki Yokoyama, Mayumi Kanagawa, John Chrzas, Seiki Baba, Yoshihiro Agari, Takashi Kumasaka, Noriko Nakagawa, Gen Ichi Sampei
Publikováno v:
Acta Crystallographica Section F Structural Biology Communications. 72:627-635
The crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, fromThermus thermophilus,Sulfolobus tokodaiiandMethanocaldococcus jannaschiiwere determined and their structural characteristics were analyzed. For Pu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b7d6781a8bc7640df68f7d3c85f07db
https://doi.org/10.1107/s2053230x1600978x
https://doi.org/10.1107/s2053230x1600978x
Autor:
Akio Ebihara, Seiki Kuramitsu, Seiki Baba, Yuzo Watanabe, Mayumi Kanagawa, Shigeyuki Yokoyama, Noriko Nakagawa, Gota Kawai, Gen-ichi Sampei
Publikováno v:
Journal of biochemistry. 159(3)
Crystal structures of 5-aminoimidazole ribonucleotide (AIR) synthetase, also known as PurM, from Thermus thermophilus (Tt) and Geobacillus kaustophilus (Gk) were determined. For TtPurM, the maximum resolution was 2.2 A and the space group was P21212
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4eaf5683470110d03f333dc176897a4d
https://pubmed.ncbi.nlm.nih.gov/26515187
https://pubmed.ncbi.nlm.nih.gov/26515187
Autor:
Mayumi Kanagawa, Shinji Fujiwara, Yoko Fukai, Hiroya Kawai, Gen-ichi Sampei, Toshiaki Shimasaki, Yuki Yanagida, Noriko Nakagawa, Shohei Mitsui, Hiroyuki Taka, Sakiko Suzuki, Shigeyuki Yokoyama, Mayumi Kusano, Seiki Kuramitsu, Gota Kawai, Kayoko Terao, Seiki Baba, Akio Ebihara
Publikováno v:
Journal of biochemistry. 154(6)
The crystal structures of glycinamide ribonucleotide transformylases (PurNs) from Aquifex aeolicus (Aa), Geobacillus kaustophilus (Gk) and Symbiobacterium toebii (St), and of formyltetrahydrofolate hydrolase (PurU) from Thermus thermophilus (Tt) were
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::396bf6d14c3a08e12c28820affccf1c3
https://pubmed.ncbi.nlm.nih.gov/24108189
https://pubmed.ncbi.nlm.nih.gov/24108189
Autor:
Gota Kawai, Hisaaki Yanai, Satoko Tamura, Seiki Baba, Kyotaro Fuse, Mayumi Kanagawa, Yuzo Watanabe, Sakiko Suzuki, Gen-ichi Sampei
Publikováno v:
Acta crystallographica. Section F, Structural biology and crystallization communications. 68(Pt 1)
The crystal structure of PurL from Thermus thermophilus HB8 (TtPurL; TTHA1519) was determined in complex with an adenine nucleotide, PO(4)(3-) and Mg(2+) at 2.35 Å resolution. TtPurL consists of 29 α-helices and 28 β-strands, and one loop is disor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94c7ec8a049e061135a628a601800a57
https://pubmed.ncbi.nlm.nih.gov/22232163
https://pubmed.ncbi.nlm.nih.gov/22232163
Autor:
Hisaaki Yanai, Seiki Baba, Mayumi Kanagawa, Noriko Nakagawa, Yoko Fukai, Akio Ebihara, Gota Kawai, Hiroya Kawai, Takeshi Ishii, Gen-ichi Sampei
Publikováno v:
Journal of biochemistry. 148(4)
Glycinamide ribonucleotide synthetase (GAR-syn, PurD) catalyses the second reaction of the purine biosynthetic pathway; the conversion of phosphoribosylamine, glycine and ATP to glycinamide ribonucleotide (GAR), ADP and Pi. In the present study, crys
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74618b3028b515fb11e028ca893cc11d
https://pubmed.ncbi.nlm.nih.gov/20716513
https://pubmed.ncbi.nlm.nih.gov/20716513
Autor:
Gen-ichi Sampei, Ryosuke Mega, Akio Ebihara, Mayumi Kanagawa, Seiki Kuramitsu, Akeo Shinkai, Gota Kawai, Ken Hirotsu, Seiki Baba, Kwang Kim
Publikováno v:
Acta crystallographica. Section F, Structural biology and crystallization communications. 66(Pt 8)
Hypoxanthine-guanine phosphoribosyltransferase (HGPRTase), which is a key enzyme in the purine-salvage pathway, catalyzes the synthesis of IMP or GMP from alpha-D-phosphoribosyl-1-pyrophosphate and hypoxanthine or guanine, respectively. Structures of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::785bde43b777eee6b0e1895e833bc622
https://pubmed.ncbi.nlm.nih.gov/20693661
https://pubmed.ncbi.nlm.nih.gov/20693661
Autor:
Takuji Suzuki, Nobuhisa Furuya, Kiyoshi Mizobuchi, Keiko Tachibana, Teruya Komano, Yasuhiro Saitou, Gen-ichi Sampei
Publikováno v:
Plasmid. 64(2)
A streptomycin and tetracycline resistance plasmid R64 isolated from Salmonella enterica serovar Typhimurium belongs to the incompatibility group I1 (IncI1). The DNA sequence of the R64 conjugative transfer region was described previously ( Komano et
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::660c9b1919ec4974dbc231cb4aa5289c
https://pubmed.ncbi.nlm.nih.gov/20594994
https://pubmed.ncbi.nlm.nih.gov/20594994