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首页> 美国卫生研究院文献>Plant Physiology >3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase Activity in Ochromonas malhamensis
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3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase Activity in Ochromonas malhamensis

机译：淡色色狼中的3-羟基-3-甲基戊二酰辅酶A还原酶活性

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摘要

3-Hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, the key regulatory enzyme of the isoprenoid pathway, was found to be predominantly microsomal in Ochromonas malhamensis, a chrysophytic alga. Detection of HMG-CoA reductase requires the presence of 1% bovine serum albumin during cell homogenization, and the activity is stimulated by the presence of Triton X-100. The enzyme has a pH optimum of 8.0 and an absolute requirement for NADPH. When grown in 10 micromolar mevinolin, a competitive inhibitor of HMG-CoA reductase, O. malhamensis shows a 10- to 15-fold increase in HMG-CoA reductase activity (after washing) with little or no effect on cell growth rate. Cultures can be maintained in 10 micromolar mevinolin for months. O. malhamensis produces a large amount (1% dry weight) of poriferasterol, a product of the isoprenoid pathway. The addition of 10 micromolar mevinolin initially blocked poriferasterol biosynthesis by >90%; within 2 days the rate of synthesis returned to normal levels. Immediately after mevinolin was washed from the 2-day culture, there was a transient 2.5-fold increase in the rate of poriferasterol biosynthesis. The rate of poriferasterol biosynthesis and the level of HMG-CoA reductase activity both fell to control levels within hours.
机译：3-hydroxy-3-methylglutaryl辅酶A（HMG-CoA）还原酶，类异戊二烯途径的关键调节酶，被发现主要是在嗜藻藻Ochromonas malhamensis中的微粒体。检测HMG-CoA还原酶需要在细胞均质化过程中存在1％的牛血清白蛋白，而Triton X-100的存在会刺激其活性。该酶的最适pH为8.0，是NADPH的绝对要求。当在10微摩尔mevinolin（一种HMG-CoA还原酶的竞争性抑制剂）中生长时，O。malhamensis显示HMG-CoA还原酶活性（洗涤后）增加了10至15倍，而对细胞生长速度的影响很小或没有影响。培养物可以在10微摩尔的mevinolin中维持数月。 O. malhamensis生产大量（1％干重）的卟啉甾醇，是类异戊二烯途径的产物。最初加入10摩尔微摩尔的甲氧萘丁醇会阻止卟啉甾醇的生物合成> 90％； 2天内合成速率恢复到正常水平。从2天的培养物中洗涤出mevinolin后，立即提高了紫杉醇生物合成速率的2.5倍瞬时增加。卟啉甾醇的生物合成速率和HMG-CoA还原酶活性水平在数小时内均降至控制水平。

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