Glycerol metabolism in higher plants: glycerol kinase |
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| Authors: | D Sadava K Moore |
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| Affiliation: | 1. Centro de Biotecnología Vegetal, Facultad de Ciencias Biológicas, Universidad Andres Bello, República 217, Santiago, Chile;2. Departamento de Acuicultura y Recursos Agroalimentarios, Universidad de Los Lagos, Fuchslocher 1305, Osorno, Chile;3. Horticulture and Product Physiology, Wageningen University, Droevendaalsesteeg 1, 6708 PD Wageningen, The Netherlands;4. Laboratorio Biorremediación, Departamento de Ciencias Forestales, Facultad de Ciencias Agropecuarias y Forestales, Universidad de La Frontera, Francisco Salazar1145, Temuco, Chile;1. Department of pharmaceutical Biochemistry, Kyung Hee University, Seoul, Republic of Korea;2. Department of Life and Nanopharmaceutical Science, Kyung Hee University, Seoul, Republic of Korea;3. Reactive Oxygen Species Medical Research Center, School of Medicine, Kyung Hee University, Republic of Korea;4. Department of Pharmacology, College of Oriental Medicine, Sangji University, Wonju-si, Gangwon-do 220-702, Republic of Korea;5. Highland Agriculture Research Center, NICS, RDA, Pyeongchang 232-955, Republic of Korea;1. Department of Anesthesiology and Intensive Care, Changhai Hospital, Second Military Medical University, Shanghai, China;2. Department of Gastroenterology, Changhai Hospital, Second Military Medical University, Shanghai, China;3. Department of Anesthesiology and Intensive Care, Shanghai Ninth People''s Hospital, Shanghai Jiaotong University, Shanghai, China |
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| Abstract: | Glycerol kinase activity was identified in extracts of higher plant seeds and seedlings, and was partially purified and characterized from cucumber radicle tissue. The enzyme was localized in the post-mitochondrial supernatant of the cell, and catalyzed the formation of glycerol-3-phosphate. The pH optiumum was 9.0. ATP, CTP, GTP or UTP could be used as the phosphoryl group donor. The Km for glycerol was 55 microM and Km values for the nucleoside triphosphates were 145-620 microM. The Vmax for the reaction was 40-78 pmol product per min. Kinetic data indicate that the enzyme has a sequential mechanism. |
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