Suppr超能文献

大鼠肝脏线粒体柠檬酸合酶的动力学特性。

The kinetic properties of citrate synthase from rat liver mitochondria.

作者信息

Shepherd D, Garland P B

出版信息

Biochem J. 1969 Sep;114(3):597-610. doi: 10.1042/bj1140597.

Abstract
  1. Citrate synthase (EC 4.1.3.7) was purified 750-fold from rat liver. 2. Measurements of the Michaelis constants for the substrates of citrate synthase gave values of 16mum for acetyl-CoA and 2mum for oxaloacetate. Each value is independent of the concentration of the other substrate. 3. The inhibition of citrate synthase by ATP, ADP and AMP is competitive with respect to acetyl-CoA. With respect to oxaloacetate the inhibition by AMP is competitive, but the inhibition by ADP and ATP is mixed, being partially competitive. 4. At low concentrations of both substrates the inhibition by ATP is sigmoidal and a Hill plot exhibits a slope of 2.5. 5. The pH optimum of the enzyme is 8.7, and is not significantly affected by ATP. 6. Mg(2+) inhibits citrate synthase slightly, but relieves the inhibition caused by ATP in a complex manner. 7. At constant total adenine nucleotide concentration made up of various proportions of ATP, ADP and AMP, the activity of citrate synthase is governed by the concentration of the sum of the energy-rich phosphate bonds of ADP and ATP. 8. The sedimentation coefficient of the enzyme, as measured by activity sedimentation, is 6.3s, equivalent to molecular weight 95000.
摘要
  1. 柠檬酸合酶(EC 4.1.3.7)从大鼠肝脏中纯化了750倍。2. 对柠檬酸合酶底物的米氏常数测量得出,乙酰辅酶A的值为16μM,草酰乙酸的值为2μM。每个值都与另一种底物的浓度无关。3. ATP、ADP和AMP对柠檬酸合酶的抑制作用相对于乙酰辅酶A是竞争性的。相对于草酰乙酸,AMP的抑制作用是竞争性的,但ADP和ATP的抑制作用是混合型的,部分为竞争性。4. 在两种底物浓度较低时,ATP的抑制作用呈S形,希尔图显示斜率为2.5。5. 该酶的最适pH为8.7,且不受ATP的显著影响。6. Mg(2+)对柠檬酸合酶有轻微抑制作用,但以复杂的方式缓解ATP引起的抑制。7. 在由不同比例的ATP、ADP和AMP组成的恒定总腺嘌呤核苷酸浓度下,柠檬酸合酶的活性受ADP和ATP中高能磷酸键总和浓度的控制。8. 通过活性沉降测量,该酶的沉降系数为6.3s,相当于分子量95000。

相似文献

引用本文的文献

本文引用的文献

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验