Chmara H, Zähner H, Borowski E
J Antibiot (Tokyo). 1984 Sep;37(9):1038-43. doi: 10.7164/antibiotics.37.1038.
Glucosamine-6-phosphate synthetase from Escherichia coli K-12 is progressively inactivated L-beta-(2,3-epoxycyclohexyl-4-on)alanine (anticapsin). With increasing concentrations of anticapsin the reaction exhibits rate saturation: the minimum inactivation half-time is 1.15 minutes, with a Kin alpha ct of 2.5 microM. Glutamine and competitive inhibitors protect against inactivation. Fructose-6-phosphate promotes the inactivation rate. It is concluded that anticapsin is an active-site directed glutamine analog in the reaction catalyzed by glucosamine-6-phosphate synthetase.
来自大肠杆菌K-12的葡糖胺-6-磷酸合成酶会被L-β-(2,3-环氧环己基-4-酮)丙氨酸（抗荚膜菌素）逐渐灭活。随着抗荚膜菌素浓度的增加，反应呈现出速率饱和：最小灭活半衰期为1.15分钟，Kin alpha ct为2.5微摩尔。谷氨酰胺和竞争性抑制剂可防止灭活。6-磷酸果糖可促进灭活速率。得出的结论是，在葡糖胺-6-磷酸合成酶催化的反应中，抗荚膜菌素是一种活性位点导向的谷氨酰胺类似物。
