• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

完全竞争性酶反应的时间相关封闭形式解。

Time-dependent closed form solutions for fully competitive enzyme reactions.

作者信息

Schnell S, Mendoza C

机构信息

Centre for Mathematical Biology, Mathematical Institute, Oxford, U.K.

出版信息

Bull Math Biol. 2000 Mar;62(2):321-36. doi: 10.1006/bulm.1999.0156.

DOI:10.1006/bulm.1999.0156
PMID:10824432
Abstract

An analytic formalism developed earlier to describe the time evolution of the basic enzyme reaction is extended to fully competitive systems. Time-dependent closed form solutions are derived for the three nominal cases of competition: even, slow and fast inhibitors, allowing for the first time the complete characterization of the reactions. In agreement with previous work, the time-independent Michaelis-Menten approach is shown to be inaccurate when a fast inhibitor is present. The validity of the quasi-steady-state approximation on which the present framework is based is also revised.

摘要

先前开发的用于描述基本酶反应时间演化的分析形式主义被扩展到完全竞争系统。针对三种典型竞争情况(即均匀、慢速和快速抑制剂)推导了随时间变化的封闭形式解,首次实现了对反应的完整表征。与先前的工作一致,当存在快速抑制剂时,与时间无关的米氏方法被证明是不准确的。还对本框架所基于的准稳态近似的有效性进行了修正。

相似文献

1
Time-dependent closed form solutions for fully competitive enzyme reactions.完全竞争性酶反应的时间相关封闭形式解。
Bull Math Biol. 2000 Mar;62(2):321-36. doi: 10.1006/bulm.1999.0156.
2
The total quasi-steady-state approximation for fully competitive enzyme reactions.完全竞争性酶反应的总准稳态近似法
Bull Math Biol. 2007 Jan;69(1):433-57. doi: 10.1007/s11538-006-9136-2. Epub 2006 Jul 19.
3
Enzyme kinetics at high enzyme concentration.高酶浓度下的酶动力学
Bull Math Biol. 2000 May;62(3):483-99. doi: 10.1006/bulm.1999.0163.
4
Stochastic chemical kinetics and the total quasi-steady-state assumption: application to the stochastic simulation algorithm and chemical master equation.随机化学动力学与总准稳态假设:应用于随机模拟算法和化学主方程。
J Chem Phys. 2008 Sep 7;129(9):095105. doi: 10.1063/1.2971036.
5
Theory and simulation of diffusion-controlled Michaelis-Menten kinetics for a static enzyme in solution.溶液中静态酶的扩散控制米氏动力学理论与模拟
J Phys Chem B. 2008 May 15;112(19):5977-87. doi: 10.1021/jp075941d. Epub 2008 Jan 26.
6
Explicit analytic approximations for time-dependent solutions of the generalized integrated Michaelis-Menten equation.广义积分米氏方程时间相关解的显式解析逼近。
Anal Biochem. 2011 Apr 15;411(2):303-5. doi: 10.1016/j.ab.2011.01.016. Epub 2011 Jan 15.
7
Generalized theoretical and practical treatment of the kinetics of an enzyme-catalyzed reaction in the presence of an enzyme equimolar irreversible inhibitor.在存在等摩尔不可逆酶抑制剂的情况下,酶催化反应动力学的广义理论与实践处理
J Chem Inf Comput Sci. 2003 Sep-Oct;43(5):1486-93. doi: 10.1021/ci0304021.
8
Michaelis-Menten kinetics at high enzyme concentrations.高酶浓度下的米氏动力学。
Bull Math Biol. 2003 Nov;65(6):1111-29. doi: 10.1016/S0092-8240(03)00059-4.
9
Quasi-steady-state kinetics at enzyme and substrate concentrations in excess of the Michaelis-Menten constant.在酶和底物浓度超过米氏常数时的准稳态动力学。
J Theor Biol. 2007 Apr 21;245(4):737-48. doi: 10.1016/j.jtbi.2006.12.005. Epub 2006 Dec 12.
10
Reactant stationary approximation in enzyme kinetics.酶动力学中的反应物稳态近似法。
J Phys Chem A. 2008 Sep 18;112(37):8654-8. doi: 10.1021/jp8026226. Epub 2008 Aug 20.

引用本文的文献

1
Theory on the rate equations of Michaelis-Menten type enzyme kinetics with competitive inhibition.米氏型酶动力学的 Michaelis-Menten 型速率方程的理论与竞争性抑制。
PLoS One. 2024 Jul 18;19(7):e0302679. doi: 10.1371/journal.pone.0302679. eCollection 2024.
2
Conversion of Similar Xenochemicals to Dissimilar Products: Exploiting Competing Reactions in Whole-Cell Catalysis.相似 Xenochemicals 向不同产物的转化:利用全细胞催化中的竞争反应。
Molecules. 2023 Jul 1;28(13):5157. doi: 10.3390/molecules28135157.
3
Identifiability of enzyme kinetic parameters in substrate competition: a case study of CD39/NTPDase1.
鉴定酶动力学参数在底物竞争中的可识别性:以 CD39/NTPDase1 为例。
Purinergic Signal. 2024 Jun;20(3):257-271. doi: 10.1007/s11302-023-09942-1. Epub 2023 May 11.
4
The quasi-steady-state approximations revisited: Timescales, small parameters, singularities, and normal forms in enzyme kinetics.重新审视准稳态近似:酶动力学中的时间尺度、小参数、奇点和规范形式。
Math Biosci. 2020 Jul;325:108339. doi: 10.1016/j.mbs.2020.108339. Epub 2020 Mar 14.
5
A theory of reactant-stationary kinetics for a mechanism of zymogen activation.酶原激活机制的反应物静止动力学理论。
Biophys Chem. 2018 Nov;242:34-44. doi: 10.1016/j.bpc.2018.08.003. Epub 2018 Aug 23.
6
Determining enzyme kinetics for systems biology with nuclear magnetic resonance spectroscopy.利用核磁共振光谱法确定系统生物学中的酶动力学。
Metabolites. 2012 Nov 6;2(4):818-43. doi: 10.3390/metabo2040818.
7
On the reducible character of Haldane-Radić enzyme kinetics to conventional and logistic Michaelis-Menten models.Haldane-Radić 酶动力学对传统和逻辑斯谛 Michaelis-Menten 模型的可约性。
Molecules. 2011 Apr 13;16(4):3128-45. doi: 10.3390/molecules16043128.