Koshiba T
Biochim Biophys Acta. 1978 Jan 12;522(1):10-8. doi: 10.1016/0005-2744(78)90317-0.
Two associated enzymes, 3-dehydroquinate hydro-lyase (EC 4.2.1.10) and shikimate:NADP+ oxidoreductase (EC 1.1.1.25), have been purified from Phaseolus mungo seedlings. These enzymes were purified 6900- and 9700-fold, respectively, but they were not separable. Moreover, two activity bands of the shikimate:NADP+ oxidoreductase were detected after polyacrylamide gel electrophoresis and the two peaks also have 3-dehydroquinate hydro-lyase activity. The two forms of the associated enzymes showed only small differences in molecular weight, Km value, pH optimum and the responses to some inhibitors.
已从绿豆幼苗中纯化出两种相关酶,即3-脱氢奎尼酸水解酶(EC 4.2.1.10)和莽草酸:NADP +氧化还原酶(EC 1.1.1.25)。这两种酶分别被纯化了6900倍和9700倍,但它们无法分离。此外,聚丙烯酰胺凝胶电泳后检测到莽草酸:NADP +氧化还原酶的两条活性带,并且这两个峰也具有3-脱氢奎尼酸水解酶活性。这两种相关酶的两种形式在分子量、Km值、最适pH以及对某些抑制剂的反应方面仅显示出微小差异。