MgATP对亚线粒体颗粒腺苷三磷酸酶活性的抑制作用。
MgATP-induced inhibition of the adenosine triphosphatase activity of submitochondrial particles.
作者信息
Lowe P N, Beechey R B
出版信息
Biochem J. 1981 May 15;196(2):443-9. doi: 10.1042/bj1960443.
Abstract
- The ATP-hydrolytic activity of ox heart submitochondrial particles can be increased from 2-3 mumol/min per mg of protein to 10-12 mumol/min per mg of protein by incubation in media containing 50 mM-Na2B4O7. This process appears to be due to the partial release of inhibitor protein from the particles. 2. The ATPase activity of submitochondrial particles can be inhibited by incubation with the substrate, MgATP. This inhibition is not due to the accumulation of the hydrolysis products, MgADP and Pi, but could involve the process of ATP hydrolysis. 3. The mechanism of MgATP-induced inhibition of ATPase activity is proposed to involve a conformational change in one of the intermediate enzyme species of the ATP-hydrolytic sequence. 4. MgATP inhibits the ATPase activity of control submitochondrial particles at a higher rate and to a greater extent than it does that of inhibitor-protein-depleted submitochondrial particles, suggesting that the conformational change involves the endogenous inhibitor protein.
摘要
- 通过在含有50 mM - Na2B4O7的培养基中孵育，牛心亚线粒体颗粒的ATP水解活性可从每毫克蛋白质2 - 3 μmol/分钟提高到每毫克蛋白质10 - 12 μmol/分钟。这个过程似乎是由于抑制剂蛋白从颗粒中部分释放所致。2. 亚线粒体颗粒的ATP酶活性可通过与底物MgATP孵育而受到抑制。这种抑制不是由于水解产物MgADP和Pi的积累，而是可能涉及ATP水解过程。3. 提出MgATP诱导ATP酶活性抑制的机制涉及ATP水解序列中一种中间酶物种的构象变化。4. MgATP对对照亚线粒体颗粒ATP酶活性的抑制速率更高、程度更大，比其对去除抑制剂蛋白的亚线粒体颗粒的抑制作用更强，这表明构象变化涉及内源性抑制剂蛋白。
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本文引用的文献
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A NATURALLY OCCURRING INHIBITOR OF MITOCHONDRIAL ADENOSINE TRIPHOSPHATASE.一种天然存在的线粒体腺苷三磷酸酶抑制剂。
J Biol Chem. 1963 Nov;238:3762-9.
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