Dehydrodolichyl diphosphate synthetase from rat seminiferous tubules |
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| Authors: | T Baba C Morris C M Allen |
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| Affiliation: | 1. Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8601, Japan;2. Department of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, 525-8577, Japan;1. State and Local Joint Engineering Laboratory for Novel Functional Polymeric Materials, College of Chemistry, Chemical Engineering and Materials Science, Soochow University, Suzhou, 215123, Jiangsu, PR China;2. NanJing YuTong Experimental School, Nanjing, 211100, Jiangsu, PR China;3. Faculty of Science, Health, Education and Engineering, University of the Sunshine Coast, Maroochydore, Queensland, 4558, Australia;4. Applied Technology College of Soochow University, Suzhou, 215325, Jiangsu, PR China;1. Institut für Theoretische Physik, Universität Heidelberg, Philosophenweg 16, 69120 Heidelberg, Germany;1. College of Life Sciences, Ritsumeikan University, Shiga 525-8577, Japan;2. Graduate School of Life Sciences, Ritsumeikan University, Shiga 525-8577, Japan;3. Research and Development Center for Marine Biosciences, Japan Agency for Marine-Earth Science and Technology, Kanagawa 237-0061, Japan;1. Department of Chemistry, Faculty of Science and Engineering, Kindai University, Higashi-Osaka, Osaka 577-8502, Japan;2. PRESTO, Japan Science and Technology Agency, Kawaguchi, Saitama 332-0012, Japan |
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| Abstract: | Homogenates of seminiferous tubules from rat testes catalyzed the incorporation of label from [14C]isopentenyl diphosphate into a variety of polyprenyl products. Long chain polyprenyl mono- and diphosphates were formed as major products when undesirable side reactions were minimized. The long chain polyprenyl diphosphate synthetase was measured as a sum of the mono- and diphosphate derivatives formed and was dependent on the addition of t,t-farnesyl diphosphate, isopentenyl diphosphate, and divalent cation. The highest activity was associated with the membranous fractions, whereas activity was negligible in the cytosolic fraction. The products of this prenyl transferase were labile to acid and yielded petroleum ether soluble products which indicated that the alpha-isoprene unit was unsaturated. Hydrolysis of either the polyprenyl mono-or diphosphates with a testicular phosphatase in the absence of NaF yielded C75, C80, C85, and C90 polyprenols. The chain lengths of the products of the synthetase suggest that this enzyme is responsible for the de novo biosynthesis of dehydrodolichyl diphosphates which are precursors of the dolichyl derivatives found in testes. |
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