兔肌肉D-3-磷酸甘油醛脱氢酶与3-磷酸甘油酸激酶相互作用的动力学证据。
Kinetic evidence for the interaction between rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase and 3-phosphoglycerate kinase.
作者信息
Sukhodolets M V, Muronetz V I, Nagradova N K
机构信息
A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, U S S R.
出版信息
Biochem Int. 1987 Aug;15(2):373-9.
The rate of 3-phosphoglycerate kinase reaction carried out under the conditions of saturating substrate concentrations (10 mM 3-phosphoglycerate, 3 mM ATP) and 0.2 mM NADH is increased in the presence of glyceraldehyde-3-phosphate dehydrogenase. This effect is probably due to the acceleration of 1.3-diphosphoglycerate transfer in the bienzyme complex (Weber and Bernhard, Biochemistry, 21,4189-4194, 1982). An analysis of the dependence of the rate constant of the coupled 3-phosphoglycerate kinase- glyceraldehyde-3-phosphate dehydrogenase reaction on the concentration of the latter enzyme was used to estimate the apparent Kd of the bienzyme complex. Under the conditions employed in this study (MOPS, 20 mM pH 7.2, 25 degrees C) this value was found to correspond to (2.5 +/- 0.6). 10(-8)M.
在底物浓度饱和（10 mM 3-磷酸甘油酸、3 mM ATP）且NADH为0.2 mM的条件下进行的3-磷酸甘油酸激酶反应速率，在甘油醛-3-磷酸脱氢酶存在时会提高。这种效应可能是由于双酶复合物中1,3-二磷酸甘油酸转移加速所致（韦伯和伯恩哈德，《生物化学》，21,4189 - 4194,1982）。通过分析偶联的3-磷酸甘油酸激酶 - 甘油醛-3-磷酸脱氢酶反应速率常数对后一种酶浓度的依赖性，来估算双酶复合物的表观解离常数。在本研究采用的条件下（20 mM MOPS，pH 7.2，25℃），发现该值对应于(2.5 ± 0.6)·10⁻⁸M。
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