• 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

变构模型中输入-输出关系的传递函数表示的有效性。

Validity of transfer-function representation of input-output relation in allosteric models.

作者信息

Sakamoto N, Naka T

出版信息

Biosystems. 1986;19(4):317-26. doi: 10.1016/0303-2647(86)90009-2.

DOI:10.1016/0303-2647(86)90009-2
PMID:3801606
Abstract

A transfer-function representation of reaction velocity is devised to describe analytically and approximately an input-output response of allosteric enzyme around a steady state. The transfer function is derived on assuming an exponential change in reaction velocity for the indicial response to substrate influx rate. The validity of the representation with variation in the kinetic parameters and flow rates is examined for the response of Koshland-Nemethy-Filmer (KNF) and Monod-Wyman-Changeux (MWC) dimeric models by comparing with the exact response obtained from the computer simulation, that is, by numerical integration of the rate equation. The representation has a wider valid region with a decrease in influx rate than with an increase. For the KNF model the representation is valid for negative cooperativity, but invalid for positive cooperativity. For the MWC model the validity decreases with stronger cooperativity. With the transfer functions valid for the Michaelis-Menten and allosteric reactions, we may derive the transfer-function representation for many metabolic pathways.

摘要

设计了反应速度的传递函数表示法,以解析并近似描述变构酶在稳态附近的输入-输出响应。该传递函数是在假设反应速度对底物流入速率的阶跃响应呈指数变化的情况下推导出来的。通过与计算机模拟得到的精确响应(即通过速率方程的数值积分)进行比较,研究了该表示法在动力学参数和流速变化时对科什兰德-内梅蒂-菲尔默(KNF)和莫诺-怀曼-尚热(MWC)二聚体模型响应的有效性。该表示法在流入速率降低时的有效区域比在流入速率增加时更宽。对于KNF模型,该表示法对负协同性有效,但对正协同性无效。对于MWC模型,有效性随协同性增强而降低。利用对米氏反应和变构反应有效的传递函数,我们可以推导出许多代谢途径的传递函数表示法。

相似文献

1
Validity of transfer-function representation of input-output relation in allosteric models.变构模型中输入-输出关系的传递函数表示的有效性。
Biosystems. 1986;19(4):317-26. doi: 10.1016/0303-2647(86)90009-2.
2
A transfer-function representation for the input-output relation in consecutive Michaelis-Menten-type reactions.
Biosystems. 1994;33(2):99-110. doi: 10.1016/0303-2647(94)90050-7.
3
Validity of quasi-steady-state and transfer-function representations for input-output relation in a Michaelis-Menten reaction.米氏反应中输入-输出关系的准稳态和传递函数表示的有效性。
Biotechnol Bioeng. 1986 Aug;28(8):1191-9. doi: 10.1002/bit.260280809.
4
A transfer-function representation for regulatory responses of a controlled metabolic pathway.
Biosystems. 1987;20(4):317-27. doi: 10.1016/0303-2647(87)90050-5.
5
Computer-based learning of cooperativity and allostery.基于计算机的协同性和变构效应学习。
Comput Appl Biosci. 1985 Sep;1(3):161-5. doi: 10.1093/bioinformatics/1.3.161.
6
Understanding allosteric and cooperative interactions in enzymes.理解酶的变构和协同相互作用。
FEBS J. 2014 Jan;281(2):621-32. doi: 10.1111/febs.12469. Epub 2013 Sep 2.
7
Structural Basis of Sequential and Concerted Cooperativity.结构基础的顺序和协同合作。
Biomolecules. 2022 Nov 7;12(11):1651. doi: 10.3390/biom12111651.
8
On the estimation of cooperativity in ion channel kinetics: activation free energy and kinetic mechanism of Shaker K+ channel.离子通道动力学中协同性的估计:Shaker K+ 通道的激活自由能和动力学机制。
J Chem Phys. 2013 Apr 28;138(16):165102. doi: 10.1063/1.4801999.
9
Kinetic cooperativity in the concerted model for allosteric enzymes.别构酶协同模型中的动力学协同性。
Biophys Chem. 1976 Mar;4(2):159-69. doi: 10.1016/0301-4622(76)85006-5.
10
[Kinetic manifestations of slow isomerization of allosteric enzyme for the model of Monod, Wyman and Changeux].[基于莫诺德、怀曼和查盖克斯模型的别构酶缓慢异构化的动力学表现]
Biokhimiia. 1975 May-Jun;40(3):611-21.

引用本文的文献

1
Statistical mechanics of Monod-Wyman-Changeux (MWC) models.莫诺-维曼-居内变换(MWC)模型的统计力学。
J Mol Biol. 2013 May 13;425(9):1433-60. doi: 10.1016/j.jmb.2013.03.013. Epub 2013 Mar 14.