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of 4
pro vyhledávání: '"Michio, Yunoki"'
Autor:
Noriaki Komoto, Ai Yamasaki, Satoshi Toyofuku, Michio Yunoki, Tsuneo Nishiki, Takahiro Sakai, Takamasa Tobimatsu, Tetsuo Toraya
Publikováno v:
Journal of Nutritional Science and Vitaminology. 53:102-108
Adenosylcobalamin-dependent diol dehydratase and glycerol dehydratase are isofunctional enzymes that catalyze the dehydration of 1,2-diols to the corresponding aldehydes. Although they bear different metabolic roles, both enzymes consist of three dif
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:
Mamoru, Yamanishi, Michio, Yunoki, Takamasa, Tobimatsu, Hideaki, Sato, Junko, Matsui, Ayako, Dokiya, Yasuhiro, Iuchi, Kazunori, Oe, Kyoko, Suto, Naoki, Shibata, Yukio, Morimoto, Noritake, Yasuoka, Tetsuo, Toraya
Publikováno v:
European journal of biochemistry. 269(18)
Recombinant glycerol dehydratase of Klebsiella pneumoniae was purified to homogeneity. The subunit composition of the enzyme was most probably alpha 2 beta 2 gamma 2. When (R)- and (S)-propane-1,2-diols were used independently as substrates, the rate
Adenosylcobalamin-dependent glycerol dehydratase undergoes inactivation by glycerol, the physiological substrate, during catalysis. In permeabilized cells of Klebsiella pneumoniae , the inactivated enzyme is reactivated in the presence of ATP, Mg 2+
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa4c8cbd23f10556f93adedd2051ed3f
https://europepmc.org/articles/PMC93905/
https://europepmc.org/articles/PMC93905/