当前位置:
X-MOL 学术
›
Bull. Korean Chem. Soc.
›
论文详情
Our official English website, www.x-mol.net, welcomes your
feedback! (Note: you will need to create a separate account there.)
Role of diffusion in the kinetics of reversible enzyme-catalyzed reactions.
Bulletin of the Korean Chemical Society ( IF 2.3 ) Pub Date : 2012-01-06 , DOI: 10.5012/bkcs.2012.33.3.925 Attila Szabo 1 , Huan-Xiang Zhou
Bulletin of the Korean Chemical Society ( IF 2.3 ) Pub Date : 2012-01-06 , DOI: 10.5012/bkcs.2012.33.3.925 Attila Szabo 1 , Huan-Xiang Zhou
Affiliation
The accurate expression for the steady-state velocity of an irreversible enzyme-catalyzed reaction obtained by Shin and co-workers is generalized to allow for the rebinding of the product. The amplitude of the power-law (t(-1/2)) relaxation of the free- and bound-enzyme concentrations to steady-state values is expressed in terms of the steady-state velocity and the intrinsic (chemical) rate constants. This result is conjectured to be exact, even though our expression for the steady-state velocity in terms of microscopic parameters is only approximate.
中文翻译:
扩散在可逆酶催化反应动力学中的作用。
Shin 及其同事获得的不可逆酶催化反应的稳态速度的准确表达被概括为允许产物的重新结合。自由和绑定酶浓度到稳态值的幂律 (t(-1/2)) 弛豫幅度用稳态速度和内在(化学)速率常数表示。尽管我们在微观参数方面对稳态速度的表达只是近似的,但这个结果被推测是准确的。
更新日期:2019-11-01
中文翻译:
扩散在可逆酶催化反应动力学中的作用。
Shin 及其同事获得的不可逆酶催化反应的稳态速度的准确表达被概括为允许产物的重新结合。自由和绑定酶浓度到稳态值的幂律 (t(-1/2)) 弛豫幅度用稳态速度和内在(化学)速率常数表示。尽管我们在微观参数方面对稳态速度的表达只是近似的,但这个结果被推测是准确的。