Khoroshilova N A, Muronetz V I, Nagradova N K
A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, USSR.
FEBS Lett. 1992 Feb 10;297(3):247-9. doi: 10.1016/0014-5793(92)80548-u.
E. coli D-glyceraldehyde-3-phosphate dehydrogenase covalently bound to Sepharose was shown to form a complex with soluble E. coli 3-phosphoglycerate kinase with a stoichiometry of 1.77 +/- 0.61 kinase molecules per tetramer of the dehydrogenase and an apparent Kd of 1.03 +/- 0.68 microM (10 mM sodium phosphate, 0.15 M NaCl). No interaction was detected between E. coli D-glyceraldehyde-3-phosphate dehydrogenase and rabbit muscle 3-phosphoglycerate kinase. The species-specificity of the bienzyme association made it possible to develop a kinetic approach to demonstrate the functionally significant interaction between E. coli D-glyceraldehyde-3-phosphate dehydrogenase and E. coli 3-phosphoglycerate kinase, which consists of an increase in steady-state rate of the coupled reaction.
已证明，与琼脂糖共价结合的大肠杆菌D-甘油醛-3-磷酸脱氢酶能与可溶性大肠杆菌3-磷酸甘油酸激酶形成复合物，其化学计量比为每四聚体脱氢酶含1.77±0.61个激酶分子，表观解离常数为1.03±0.68微摩尔（10毫摩尔磷酸钠，0.15摩尔氯化钠）。未检测到大肠杆菌D-甘油醛-3-磷酸脱氢酶与兔肌肉3-磷酸甘油酸激酶之间有相互作用。双酶结合的物种特异性使得开发一种动力学方法成为可能，以证明大肠杆菌D-甘油醛-3-磷酸脱氢酶与大肠杆菌3-磷酸甘油酸激酶之间功能上显著的相互作用，这种相互作用表现为偶联反应稳态速率的增加。
