Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Koichiro Kinoshita"'
Autor:
Aya Tanokuchi, Naoki Shibata, Hirokazu Obayashi, Takamasa Tobimatsu, Tetsuo Toraya, Koichiro Kinoshita, Masaki Fukuoka, Mamoru Yamanishi, Takuya Saito, Koichi Mori, Yuuki Ikeda
Publikováno v:
FEBS Journal. 279:793-804
Coenzyme B12 dependent diol dehydratase undergoes mechanism-based inactivation by glycerol, accompanying the irreversible cleavage of the coenzyme Co–C bond. Bachovchin et al. [Biochemistry16, 1082–1092 (1977)] reported that glycerol bound in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8c2cc0da44e7d0d5892e22a336ea8385
https://doi.org/10.1111/j.1742-4658.2012.08470.x
https://doi.org/10.1111/j.1742-4658.2012.08470.x
Publikováno v:
Journal of High Temperature Society. 36:233-239
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b6845d0cc0f4156a636800b189bbf6c5
https://doi.org/10.7791/jhts.36.233
https://doi.org/10.7791/jhts.36.233
Autor:
Mamoru Yamanishi, Ai Yamasaki, Masahiro Kawata, Noriaki Komoto, Koichiro Kinoshita, Takamasa Tobimatsu, Tetsuo Toraya, Naoki Hieda, Takeshi Watanabe, Ken Ichi Ogura
Publikováno v:
Biochemistry. 47:3162-3173
Diol dehydratase of Klebsiella oxytoca contains an essential histidine residue. Its X-ray structure revealed that the migrating hydroxyl group on C2 of substrate is hydrogen-bonded to Hisalpha143. Mutant enzymes in which Hisalpha143 was mutated to an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc5994984da0783e7ef3615965bdc444
https://doi.org/10.1021/bi7018095
https://doi.org/10.1021/bi7018095
Publikováno v:
The Proceedings of Conference of Kansai Branch. :5-15
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2dbb92fbaae49b3ecc6cf3b1ad592749
https://doi.org/10.1299/jsmekansai.2004.79._5-15_
https://doi.org/10.1299/jsmekansai.2004.79._5-15_
Autor:
Mamoru, Yamanishi, Koichiro, Kinoshita, Masaki, Fukuoka, Takuya, Saito, Aya, Tanokuchi, Yuuki, Ikeda, Hirokazu, Obayashi, Koichi, Mori, Naoki, Shibata, Takamasa, Tobimatsu, Tetsuo, Toraya
Publikováno v:
The FEBS journal. 279(5)
Coenzyme B(12) dependent diol dehydratase undergoes mechanism-based inactivation by glycerol, accompanying the irreversible cleavage of the coenzyme Co-C bond. Bachovchin et al. [Biochemistry16, 1082-1092 (1977)] reported that glycerol bound in the G
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::44077f6456ca9379605570be561ddf64
https://pubmed.ncbi.nlm.nih.gov/22221669
https://pubmed.ncbi.nlm.nih.gov/22221669
Autor:
Sumihisa Takahashi, Takamasa Tobimatsu, Tetsuo Toraya, Mamoru Yamanishi, Noriaki Komoto, Ken Ichi Ogura, Masahiro Kawata, Koichiro Kinoshita
Publikováno v:
The Journal of biological chemistry. 281(27)
The importance of each active-site residue in adenosylcobalamin-dependent diol dehydratase of Klebsiella oxytoca was estimated using mutant enzymes in which one of the residues interacting with substrate and/or K(+) was mutated to Ala or another amin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8c2b032413b552f654263fe6cb19126
https://pubmed.ncbi.nlm.nih.gov/16571729
https://pubmed.ncbi.nlm.nih.gov/16571729
Autor:
Takamitsu Yoshimoto, Koichiro Kinoshita, Taku Otoshi, Toshimi Takagi, Naoshi Kubo, Yoshiro Kato
Publikováno v:
The Proceedings of the Thermal Engineering Conference. 2003:31-32
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fe275ca0822e4c7cde2731cc391cac98
https://doi.org/10.1299/jsmeted.2003.31
https://doi.org/10.1299/jsmeted.2003.31
Publikováno v:
The Proceedings of Conference of Kansai Branch. :9-7
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4642adef2c30130dd0e94ffb00b62695
https://doi.org/10.1299/jsmekansai.2003.78._9-7_
https://doi.org/10.1299/jsmekansai.2003.78._9-7_