粗糙脉孢菌五功能芳香酶复合物的3-脱氢奎尼酸合酶活性依赖于Zn2+。
The 3-dehydroquinate synthase activity of the pentafunctional arom enzyme complex of Neurospora crassa is Zn2+-dependent.
作者信息
Lambert J M, Boocock M R, Coggins J R
出版信息
Biochem J. 1985 Mar 15;226(3):817-29. doi: 10.1042/bj2260817.
Abstract
We have demonstrated the co-purification in constant ratio of all five activities of the pentafunctional arom enzyme complex from Neurospora crassa. Progressive inactivation of the 3-dehydroquinate synthase component of the purified enzyme complex by chelating agents was blocked by the substrate, 3-deoxy-D-arabino-heptulosonate 7-phosphate, but not by the cofactor NAD+. Full activity was restored at Zn2+ concentrations as low as 0.05 nM. Atomic absorption data indicated that the intact enzyme complex contained 1 atom per subunit of tightly bound zinc. The arom 3-dehydroquinate synthase had a calculated turnover number of 19s-1, this being within the narrow range of values obtained for the other four activities of the intact multifunctional enzyme. The Km for 3-deoxy-D-arabino-heptulosonate 7-phosphate was 1.4 microM in a phosphate-free buffer; inorganic phosphate was a competitive inhibitor with respect to 3-deoxy-D-arabino-heptulosonate 7-phosphate.
摘要
我们已经证明，来自粗糙脉孢菌的五功能芳香酶复合物的所有五种活性以恒定比例共纯化。螯合剂对纯化酶复合物的3-脱氢奎尼酸合酶组分的逐步失活被底物3-脱氧-D-阿拉伯庚糖酸7-磷酸阻断，但不被辅因子NAD +阻断。在低至0.05 nM的Zn2 +浓度下恢复了全部活性。原子吸收数据表明，完整的酶复合物每个亚基含有1个紧密结合的锌原子。芳香3-脱氢奎尼酸合酶的计算周转数为19s-1，这在完整多功能酶的其他四种活性所获得的值的狭窄范围内。在无磷酸盐缓冲液中，3-脱氧-D-阿拉伯庚糖酸7-磷酸的Km为1.4 microM；无机磷酸盐是3-脱氧-D-阿拉伯庚糖酸7-磷酸的竞争性抑制剂。
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