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Miyamoto, E., Tanioka, Y., Nishizawa-Yokoi, A., Yabuta, Y., Ohnishi, K., Nisono, H., Shigeoka, S., Nakano, Y. and Watanabe, F. (2010) Characterization of Methylmalonyl-CoA Mutase Involved in the Propionate Photoassimilation of Euglena gracilis Z. Archives of Microbiology, 192, 437-446.
http://dx.doi.org/10.1007/s00203-010-0572-x

has been cited by the following article:

• TITLE: Dodecylamine Derivative of Hydroxocobalamin Acts as a Potent Inhibitor of Cobalamin-Dependent Methionine Synthase in Mammalian Cultured COS-7 Cells

  AUTHORS: Tomohiro Bito, Mariko Yasui, Toshio Iwaki, Yukinori Yabuta, Tsuyoshi Ichiyanagi, Ryoichi Yamaji, Yoshihisa Nakano, Hiroshi Inui, Fumio Watanabe

  KEYWORDS: Dodecylamine Derivative, Cobalamin, COS-7 Cell, Enzyme Inhibitor, Hydroxocobalamin

  JOURNAL NAME: Food and Nutrition Sciences, Vol.5 No.14, August 6, 2014

  ABSTRACT: We evaluated whether the dodecylamine derivative of hydroxocobalamin acts as a potent inhibitor of cobalamin-dependent enzymes in an African green monkey kidney cell, COS-7. When the dodecylamine derivative (1.0 μmol/L) did not show any cytotoxicity in the cultured cells, the derivative could not affect methylmalonyl-CoA mutase (holo-enzyme) activity, but significantly inhibit methionine synthase (holo-enzyme) activity in the cell homogenates of COS-7 grown in 1.0 μmol/L hydroxocobalamin-supplemented medium. An immunoblot analysis indicated that the dodecylamine derivative could not decrease the protein level of methionine synthase, but significantly inhibit the enzyme activity.