Author(s)

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

Department of Clinical Nutrition, Osaka Prefecture University, Habikino, Japan.
Division of Applied Biological Chemistry, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Sakai, Japan.
Division of Applied Biological Chemistry, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Sakai, Japan; Department of Clinical Nutrition, Osaka Prefecture University, Habikino, Japan.
Division of Applied Biological Chemistry, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Sakai, Japan; Department of Life Science, Osaka Women’s Junior College, Fujiidera, Japan.
Division of Applied Bioresources Chemistry, The United Graduate School of Agricultural Sciences, Tottori University, Tottori, Japan.

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.

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

Bito, T. , Yasui, M. , Iwaki, T. , Yabuta, Y. , Ichiyanagi, T. , Yamaji, R. , Nakano, Y. , Inui, H. and Watanabe, F. (2014) Dodecylamine Derivative of Hydroxocobalamin Acts as a Potent Inhibitor of Cobalamin-Dependent Methionine Synthase in Mammalian Cultured COS-7 Cells. Food and Nutrition Sciences, 5, 1318-1325. doi: 10.4236/fns.2014.514143.