d-Aspartate N-methyltransferase catalyzes biosynthesis of N-methyl-d-aspartate (NMDA), a well-known selective agonist of the NMDA receptor,in mice |
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| Institution: | 1. Research Reactor Institute, Kyoto University Kumatori-cho, Sennan-gun, Osaka 590-0494, Japan;2. Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan;3. Shimazu Corporation, Sakyo-ku, Kyoto 606-8502, Japan;1. Graduate School of Pharmaceutical Sciences, Kyushu University, 3-1-1 Maidashi, Higasi-ku, Fukuoka 812-8582, Japan;2. KAGAMI Inc., 7-7-15 Saito-asagi, Ibaraki 567-0085, Japan;3. Department of Earth and Planetary Sciences, Kyushu University, 744 Motooka, Nishi-ku, Fukuoka 819-0395, Japan;1. Laboratory of Biochemistry, Faculty of Science, Kochi University, Kochi 780-8520, Japan;2. Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94158, USA;3. Department of Plant and Soil Sciences, 311 Plant Science Building, University of Kentucky, Lexington, KY 40546-0312, USA |
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| Abstract: | N-Methyl-d-aspartate (NMDA), which is a selective agonist for the NMDA receptor, has recently been shown to be present in various biological tissues. In mammals, the activity of d-aspartate N-methyltransferase (DDNMT), which produces NMDA from d-aspartate, has been detected only in homogenates prepared from rat tissues. Moreover, the enzymatic properties of DDNMT have been poorly studied and its molecular entity has not yet been identified. In this report, we show for the first time that the activity of DDNMT is present in mouse tissues and succeed in obtaining a partially purified enzyme preparation from a mouse tissue homogenate with a purification fold of 1900 or more, and have characterized the enzymatic activity of this preparation. The results indicate that DDNMT, which is highly specific for d-aspartate and is S-adenosyl-l-methionine-dependent, is a novel enzyme that clearly differs from the known methylamine-glutamate N-methyltransferase (EC 2.1.1.21) and glycine N-methyltransferase (EC 2.1.1.20). |
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