作者: Andreas Portsteffen , Birgit Draeger , Adolf Nahrstedt
DOI: 10.1016/0031-9422(92)80247-C
关键词: Stereochemistry 、 Enzyme 、 Cofactor 、 Hyoscyamus niger 、 Biology 、 Tropine 、 Datura stramonium 、 Tropinone 、 Affinity chromatography 、 Enzyme assay 、 Biochemistry
摘要: Abstract Two different tropinone reductases (TR) were isolated from transformed root cultures of Datura stramonium. Both activities completely separated by hydrophobic interaction chromatography and affinity chromatography. Gas chromatographic analysis the reaction products showed one enzyme activity forming tropine only (TR I) other exclusively pseudotropine II). TR I after extraction purification about five-fold II. Characterization both enzymes revealed differences to previously stramonium, D. innoxia Hyoscyamus niger, between individual proteins. a pronounced pH-dependency while II was more tolerant pH-values. accepted NADPH as coenzyme; Km values 1.39 mM 0.22 II) for 59 μM 17 NADPH.