Purification and some properties of discadenine synthase from Dictyostelium discoideum |
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| Affiliation: | 1. Institute of Biological Sciences, University of Tsukuba, Ibaraki 305, Japan;2. Biology Division, National Cancer Center Research Institute, Tsukiji, Chuoku, Tokyo 104, Japan;1. Department of Chemistry, Faculty of Mathematics and Natural Sciences, Padjadjaran University, Jatinangor 45363, Indonesia;2. Department of Chemistry, Faculty of Science, University of Malaya, Kuala Lumpur 59100, Malaysia;3. Division of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Gakuen-cho, Sakai, Osaka 599-8531, Japan |
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| Abstract: | The enzyme discadenine synthase, which transfers the 3-amino-3-carboxypropyl residue of S-adenosylmethionine to an acceptor, N6-isopentenyladenine, from the fruiting body of the cellular slime mold Dictyostelium discoideum, was purified 420-fold. Its apparent molecular mass was 82 000 Da and the isoelectric point was pH 5.8. The Km value for S-adenosylmethionine was 1.85 · 10−5 M and for benzyladenine was 7.0 · 10−7 M. In contrast to theenzyme which catalyzes the formation of 3-(3-amino-3-carboxypropyl)uridine in tRNAs, the present enzyme did not require Mg2+ and was not stimulated by ATP. Some other metal ions (Zn2+, Mn2+, Ca2+) showed inhibition at 10–100 mM. |
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