Hawkes T R, Lewis T, Coggins J R, Mousdale D M, Lowe D J, Thorneley R N
I.C.I. Agrochemical, Jcalotts Hill Research Station, Bracknell, Berks, U.K.
Biochem J. 1990 Feb 1;265(3):899-902. doi: 10.1042/bj2650899.
The pre-steady-state kinetics of phosphate formation from 5-enolpyruvylshikimate 3-phosphate catalysed by Escherichia coli chorismate synthase (EC 4.6.1.4) were studied by a rapid-acid-quench technique at 25 degrees C at pH 7.5. No pre-steady-state 'burst' or 'lag' phase was observed, showing that phosphate is released concomitant with the rate-limiting step of the enzyme. The implications of this result for the mechanism of action of chorismate synthase are discussed.
采用快速酸淬灭技术,在25℃、pH 7.5条件下,研究了大肠杆菌分支酸合酶(EC 4.6.1.4)催化5-烯醇丙酮酸莽草酸-3-磷酸生成磷酸盐的前稳态动力学。未观察到前稳态“爆发”或“滞后”阶段,表明磷酸盐的释放与该酶的限速步骤同步。讨论了这一结果对分支酸合酶作用机制的影响。