Characterization of methylglyoxal synthase in Saccharomyces cerevisiae |
| |
| Authors: | K Murata Y Fukuda K Watanabe T Saikusa M Shimosaka A Kimura |
| |
| Affiliation: | 1. Stress Molecules, Institut Jacques Monod, Université Paris 7, CNRS UMR 7592, 15 rue Hélène Brion, 75013 Paris, France;2. Institut Pasteur, Unité de Biologie Moléculaire du Gène chez les Extrêmophiles, Département de Microbiologie, F-75015, Paris, France;3. Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, Fukuoka, Japan;1. Department of Food Science, Yanbian University, Yanji, Jilin 133002, China;2. Brain Korea 21 Center for Bio-Resource Development, Division of Animal, Horticultural and Food Sciences, Chungbuk National University, Cheongju 361-763, South Korea;3. Department of Milk Processing Research Team, Korea Yakult, Youngin 446-901, South Korea;1. Department of Chemistry, University of Washington, Seattle, WA 98195-2180, USA;2. Shandong Province Key Laboratory of Applied Mycology, School of Life Sciences, Qingdao Agricultural University, Shandong Province 266104, PR China;3. Key Laboratory of Systems Bioengineering, Ministry of Education, Tianjin University, Tianjin 300072, PR China;4. Department of Chemical Engineering, University of Washington, Seattle, WA 98195-2180, USA;5. Department of Microbiology, University of Washington, Seattle, WA 98195-2180, USA |
| |
| Abstract: | Methylglyoxal synthase in Saccharomyces cerevisiae was purified approximately 300 folds from cell extracts with 20% of activity yield. During purification procedures, polymorphic behaviours of the enzyme were observed. The purified enzyme was homogeneous on polyacrylamide gel electrophoresis and consisted of a single polypeptide chain of Mr = 26,000. The enzyme was most active at pH 9.5-10.5 and strictly specific to dihydroxyacetone phosphate with Km = 3 mM. Phosphoenolpyruvate, glyceraldehyde-3-phosphate, orthophosphate and thiol compounds were potent inhibitors of the enzyme. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
