ANALYSIS OF TIME-DEPENDENT CHANGE OF ESCHERICHIA-COLI F1-ATPASE ACTIVITY AND ITS RELATIONSHIP WITH APPARENT NEGATIVE COOPERATIVITY
ANALYSIS OF TIME-DEPENDENT CHANGE OF ESCHERICHIA-COLI F1-ATPASE ACTIVITY AND ITS RELATIONSHIP WITH APPARENT NEGATIVE COOPERATIVITY
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DOI：
10.1016/0005-2728(95)00087-y
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发表时间：
1995-10-10
影响因子：
4.3
通讯作者：
YOSHIDA, M
中科院分区：
文献类型：
--
作者：
KATO, Y;SASAYAMA, T;YOSHIDA, M
除了epsilon亚基解离引起EF(1)（来自大肠杆菌的f -1- atp酶）逐渐激活的情况外[Laget， P.P.和Smith， J.B. (1979) Arch。物化学。[j] .生物物理学报，1997,83 -89]，EF(1)，长期以来被认为不表现出时间依赖性的活动变化[j]。物化学。生物化学学报，1997,38(4):344 -344。在这里，我们报道了EF(1)的时间依赖性失活和激活，这显然类似于线粒体f -1- atp酶的失活和激活[Vasilyeva， E.A.等人，（1982）Biochem]。[j].科学通报，2002,15 -23。分析这些变化与负协同性相关的ATP浓度的函数表明，初始失活阶段是由于与低K-m（约10 μ M）相关的V-max降低，而随后的激活可能是由于epsilon亚基的解离，与高K-m（约100 μ M）相关的V-max增加相对应。因此，EF(1)活性的时间依赖性变化与ATP水解的明显负协同性（多个K-m值）密切相关。
Except for the case of gradual activation of EF(1) (F-1-ATPase from Escherichia coli) caused by the dissociation of the epsilon subunit [Laget, P.P. and Smith, J.B. (1979) Arch. Biochem. Biophys. 197, 83-89], EF(1) has long been thought not to show a time-dependent change in activity [Senior, A.E. et al. (1992) Arch. Biochem. Biophys. 297, 340-344]. Here, we report the time-dependent inactivation and activation of EF(1), which are apparently similar to those of mitochondrial F-1-ATPases [Vasilyeva, E.A. et al, (1982) Biochem. J. 202, 15-23]. Analysis of these changes as a function of ATP concentrations in relation to negative cooperativity revealed that the initial inactivation phase was attributable to the decrease in the V-max associated with the low K-m (around 10 mu M), and the following activation, probably due to the dissociation of the epsilon subunit, corresponded to the increase in the V-max associated with the high K-m (in the order of 100 mu M). Thus, the time-dependent change in EF(1) activity is closely related to the apparent negative cooperativity (multiple K-m values) of ATP hydrolysis.