Heilmann H D, Bürger M
Hoppe Seylers Z Physiol Chem. 1981 Dec;362(12):1567-74. doi: 10.1515/bchm2.1981.362.2.1567.
The activity of the enzyme tryptophan synthase from Escherichia coli was tested as a function of the concentration of L-serine which serves as a substrate in the indole to tryptophan reaction as well as for the L-serine deaminase activity. L-Serine binding was found to follow the pattern of negative cooperativity both by kinetic and by equilibrium methods. The enzyme kinetic data support the view that a rapid equilibration model for the enzyme . substrates complex formation is not strictly obeyed.
对来自大肠杆菌的色氨酸合酶的活性进行了测试，该活性是作为吲哚转化为色氨酸反应中底物的L-丝氨酸浓度的函数，同时也测试了其L-丝氨酸脱氨酶活性。通过动力学方法和平衡方法发现，L-丝氨酸结合呈现负协同性模式。酶动力学数据支持这样一种观点，即酶-底物复合物形成的快速平衡模型并未被严格遵守。
