Easterby J S
Department of Biochemistry, University of Liverpool, U.K.
Biochem J. 1989 Dec 1;264(2):605-7. doi: 10.1042/bj2640605.
Multienzyme complexes and multifunctional proteins may confer a kinetic advantage by channelling reaction intermediates between consecutive enzymes and reducing the transient time for the establishment of steady states. A general means for quantitatively assessing the contribution of channelling to the reduction of pool size and transient time is presented. Restrictions to the kinetic advantage are identified, and it is shown that no channelling advantage is obtained at high enzyme concentration or for enzymes which exhibit rapid-equilibrium kinetic behaviour.
多酶复合物和多功能蛋白质可以通过在连续的酶之间传递反应中间体并减少建立稳态的瞬态时间来赋予动力学优势。本文提出了一种定量评估通道化对减小库大小和瞬态时间贡献的通用方法。确定了对动力学优势的限制，并表明在高酶浓度下或对于表现出快速平衡动力学行为的酶，不会获得通道化优势。
