Zobrazeno 1 - 10
of 70
pro vyhledávání: '"Yasuyuki Kato-Yamada"'
Autor:
Miria Fujiwara, Yasuyuki Kato-Yamada
Publikováno v:
Biochemistry and Biophysics Reports, Vol 21, Iss , Pp - (2020)
The ε subunits of several bacterial F1-ATPases bind ATP. ATP binding to the ε subunit has been shown to be involved in the regulation of F1-ATPase from thermophilic Bacillus sp. PS3 (TF1). We previously reported that the dissociation constant for A
Externí odkaz:
https://doaj.org/article/e2fda21a11374c9c94438f4a22847b03
Autor:
Genki Akanuma, Tomoaki Tagana, Maho Sawada, Shota Suzuki, Tomohiro Shimada, Kan Tanaka, Fujio Kawamura, Yasuyuki Kato‐Yamada
Publikováno v:
MicrobiologyOpen, Vol 8, Iss 8, Pp n/a-n/a (2019)
Abstract The ε subunit of FoF1‐ATPase/synthase (FoF1) plays a crucial role in regulating FoF1 activity. To understand the physiological significance of the ε subunit‐mediated regulation of FoF1 in Bacillus subtilis, we constructed and character
Externí odkaz:
https://doaj.org/article/b699ae750a1b4d29b25d1eb3812f0ba8
Publikováno v:
PLoS ONE, Vol 12, Iss 5, p e0177907 (2017)
The ε subunit from bacterial ATP synthases functions as an ATP sensor, preventing ATPase activity when the ATP concentration in bacterial cells crosses a certain threshold. The R103A/R115A double mutant of the ε subunit from thermophilic Bacillus P
Externí odkaz:
https://doaj.org/article/4f255736a5f149958f5b56ed331a8d22
Autor:
Toru Ishikawa, Yasuyuki Kato-Yamada
Publikováno v:
PLoS ONE, Vol 9, Iss 9, p e107197 (2014)
F1-ATPase from Bacillus subtilis (BF1) is severely suppressed by the MgADP inhibition. Here, we have tested if this is due to the loss of nucleotide binding to the noncatalytic site that is required for the activation. Measurements with a tryptophan
Externí odkaz:
https://doaj.org/article/6fca195b332148deab3483bfd941c8a7
Autor:
Hideaki Nanamiya, Hirofumi Yoshikawa, Taku Chibazakura, Fumiya Okawa, Akiko Soma, Satoru Watanabe, Genki Akanuma, Yousuke Natori, Yasuyuki Kato-Yamada, Masaki Watanabe, Kei Asai, Fujio Kawamura, Takashi Hishida
Publikováno v:
J Bacteriol
Ribosomal protein S14 can be classified into three types. The first, the C+ type has a Zn2+ binding motif and is ancestral. The second and third are the C− short and C− long types, neither of which contain a Zn2+ binding motif and which are ca. 9
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9a62da04816e94f087256eaf6daabc5
https://doi.org/10.1128/jb.00599-20
https://doi.org/10.1128/jb.00599-20
Autor:
Junya Mizumoto, Yuka Kikuchi, Yo-Hei Nakanishi, Naoto Mouri, Anrong Cai, Tokushiro Ohta, Takamitsu Haruyama, Yasuyuki Kato-Yamada
Publikováno v:
PLoS ONE, Vol 8, Iss 8, p e73888 (2013)
MgADP inhibition, which is considered as a part of the regulatory system of ATP synthase, is a well-known process common to all F1-ATPases, a soluble component of ATP synthase. The entrapment of inhibitory MgADP at catalytic sites terminates catalysi
Externí odkaz:
https://doaj.org/article/2a8d00e2f9564c25b7ec7015e81e6a0d
Autor:
Yasuyuki Kato-Yamada, Miria Fujiwara
Publikováno v:
Biochemistry and Biophysics Reports
Biochemistry and Biophysics Reports, Vol 21, Iss, Pp-(2020)
Biochemistry and Biophysics Reports, Vol 21, Iss, Pp-(2020)
The ε subunits of several bacterial F1-ATPases bind ATP. ATP binding to the ε subunit has been shown to be involved in the regulation of F1-ATPase from thermophilic Bacillus sp. PS3 (TF1). We previously reported that the dissociation constant for A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ba5246c2abcb240482bd4683ede1be6
http://europepmc.org/articles/PMC6953521
http://europepmc.org/articles/PMC6953521
Autor:
Yasuyuki Kato-Yamada, R Makino, Yuki Hamajima, Tetsutaro Iizuka, Motonari Tsubaki, Yoshitsugu Shiro, Keisuke Mashima, Yuji Obata
Publikováno v:
Biochemistry. 57:1620-1631
Soluble guanylate cyclase (sGC) is a heme-containing enzyme that catalyzes cGMP production upon sensing NO. While the CO adduct, sGC-CO, is much less active, the allosteric regulator BAY 41-2272 stimulates the cGMP productivity to the same extent as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c0b40ac33af765b4996fce486edfb74
https://doi.org/10.1021/acs.biochem.7b01240
https://doi.org/10.1021/acs.biochem.7b01240
Publikováno v:
Biophysical Journal. 114:178-187
F1-ATPase is a rotary motor protein driven by ATP hydrolysis. Among molecular motors, F1 exhibits unique high reversibility in chemo-mechanical coupling, synthesizing ATP from ADP and inorganic phosphate upon forcible rotor reversal. The e subunit en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7d6b09b2d1d080d2213b850b23a3963c
https://doi.org/10.1016/j.bpj.2017.11.004
https://doi.org/10.1016/j.bpj.2017.11.004
Autor:
Shota Suzuki, Tomoaki Tagana, Kan Tanaka, Genki Akanuma, Tomohiro Shimada, Yasuyuki Kato-Yamada, Fujio Kawamura, Maho Sawada
Publikováno v:
MicrobiologyOpen, Vol 8, Iss 8, Pp n/a-n/a (2019)
MicrobiologyOpen
MicrobiologyOpen
The e subunit of Fo F1 -ATPase/synthase (Fo F1 ) plays a crucial role in regulating Fo F1 activity. To understand the physiological significance of the e subunit-mediated regulation of Fo F1 in Bacillus subtilis, we constructed and characterized a mu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1afa8bb7f4a529eed1272e81744d45c1
https://doaj.org/article/b699ae750a1b4d29b25d1eb3812f0ba8
https://doaj.org/article/b699ae750a1b4d29b25d1eb3812f0ba8