苏氨酸
大肠杆菌
酶
动力学
赖氨酸
生物化学
化学
代谢物
酶动力学
丝氨酸
氨基酸
活动站点
物理
量子力学
基因
作者
Christophe Chassagnole,Badr RAÏS,E Quentin,David A. Fell,Jean‐Pierre Mazat
标识
DOI:10.1042/0264-6021:3560415
摘要
We have determined the kinetic parameters of the individual steps of the threonine pathway from aspartate in Escherichia coli under a single set of experimental conditions chosen to be physiologically relevant. Our aim was to summarize the kinetic behaviour of each enzyme in a single tractable equation that takes into account the effect of the products as competitive inhibitors of the substrates in the forward reaction and also, when appropriate (e.g. near-equilibrium reactions), as substrates of the reverse reactions. Co-operative feedback inhibition by threonine and lysine was also included as necessary. We derived the simplest rate equations that describe the salient features of the enzymes in the physiological range of metabolite concentrations in order to incorporate them ultimately into a complete model of the threonine pathway, able to predict quantitatively the behaviour of the pathway under natural or engineered conditions.
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