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1
How to draw kinetic barrier diagrams for enzyme-catalysed reactions.如何绘制酶催化反应的动力学屏障图。
Biochem J. 1991 May 15;276 ( Pt 1)(Pt 1):265-8. doi: 10.1042/bj2760265.
2
The analysis of progress curves for enzyme-catalysed reactions by non-linear regression.通过非线性回归分析酶催化反应的进程曲线。
Biochim Biophys Acta. 1977 Apr 12;481(2):297-312. doi: 10.1016/0005-2744(77)90264-9.
3
Determination of the kinetic properties of enzymes catalysing coupled reaction sequences.催化偶联反应序列的酶的动力学性质的测定。
Biochim Biophys Acta. 1983 May 18;744(3):249-59. doi: 10.1016/0167-4838(83)90197-8.
4
Substrate channeling in glycolysis: a phantom phenomenon.糖酵解中的底物通道化:一种虚拟现象。
Proc Natl Acad Sci U S A. 1991 Jan 15;88(2):497-501. doi: 10.1073/pnas.88.2.497.
5
[Observation of non-equilibrium phase transitions in a closed enzyme system. Intermittent regulation of the activity of lactate dehydrogenase and similar enzymes].
Mol Biol (Mosk). 1981 Sep-Oct;15(5):1169-79.
6
[Kinetic studies of the formation of abortive ternary complex lactate dehydrogenase (isoenzyme h4)-NAD-pyruvate].[乳酸脱氢酶(同工酶h4)-烟酰胺腺嘌呤二核苷酸-丙酮酸流产性三元复合物形成的动力学研究]
Biokhimiia. 1975 Mar-Apr;40(2):281-9.
7
Macroscopic rate constants involved in the formation and interconversion of the two central enzyme--substrate complexes of the lactate dehydrogenase turnover.参与乳酸脱氢酶周转的两个核心酶 - 底物复合物形成和相互转化的宏观速率常数。
Biochem J. 1974 Apr;139(1):261-71. doi: 10.1042/bj1390261.
8
Direct transfer of NADH between alpha-glycerol phosphate dehydrogenase and lactate dehydrogenase: fact or misinterpretation?α-甘油磷酸脱氢酶与乳酸脱氢酶之间NADH的直接转移:事实还是误解?
Proc Natl Acad Sci U S A. 1989 Sep;86(17):6464-8. doi: 10.1073/pnas.86.17.6464.
9
[Simple kinetic models explaining critical phenomena in enzymatic reactions with isomerization of the enzyme and substrate].[解释酶与底物异构化的酶促反应中临界现象的简单动力学模型]
Mol Biol (Mosk). 1988 Sep-Oct;22(5):1381-92.
10
Kinetic barriers under steady-state conditions.稳态条件下的动力学屏障。
Biochem J. 1992 May 15;284 ( Pt 1)(Pt 1):213-9. doi: 10.1042/bj2840213.

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Mammalian Esterase Activity: Implications for Peptide Prodrugs.哺乳动物酯酶活性:对肽前药的影响。
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2
Control analysis applied to single enzymes: can an isolated enzyme have a unique rate-limiting step?应用于单一酶的控制分析:一种孤立的酶能有独特的限速步骤吗?
Biochem J. 1993 Aug 15;294 ( Pt 1)(Pt 1):87-94. doi: 10.1042/bj2940087.
3
Kinetic barriers under steady-state conditions.稳态条件下的动力学屏障。
Biochem J. 1992 May 15;284 ( Pt 1)(Pt 1):213-9. doi: 10.1042/bj2840213.

本文引用的文献

1
Mathematical treatment of enzyme-catalyzed isotope-exchange reactions.
Eur J Biochem. 1972 Oct;30(2):325-9. doi: 10.1111/j.1432-1033.1972.tb02101.x.
2
Macroscopic rate constants involved in the formation and interconversion of the two central enzyme--substrate complexes of the lactate dehydrogenase turnover.参与乳酸脱氢酶周转的两个核心酶 - 底物复合物形成和相互转化的宏观速率常数。
Biochem J. 1974 Apr;139(1):261-71. doi: 10.1042/bj1390261.
3
The lactate dehydrogenase--reduced nicotinamide--adenine dinucleotide--pyruvate complex. Kinetics of pyruvate binding and quenching of coeznyme fluorescence.乳酸脱氢酶-还原型烟酰胺-腺嘌呤二核苷酸-丙酮酸复合物。丙酮酸结合动力学及辅酶荧光猝灭。
Biochem J. 1974 Apr;139(1):251-9. doi: 10.1042/bj1390251.
4
Rate of isotope exchange in enzyme-catalyzed reactions.酶催化反应中的同位素交换速率。
Biochemistry. 1969 Jan;8(1):352-60. doi: 10.1021/bi00829a049.
5
Evolutionary optimization of the catalytic effectiveness of an enzyme.酶催化效率的进化优化。
Biochemistry. 1989 Nov 28;28(24):9293-305. doi: 10.1021/bi00450a009.

如何绘制酶催化反应的动力学屏障图。

How to draw kinetic barrier diagrams for enzyme-catalysed reactions.

作者信息

Südi J

机构信息

Abteilung Toxkologie, Christian-Albrechts-Universität, Kiel, Federal Republic of Germany.

出版信息

Biochem J. 1991 May 15;276 ( Pt 1)(Pt 1):265-8. doi: 10.1042/bj2760265.

DOI:10.1042/bj2760265
PMID:2039478
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1151175/
Abstract

A modified way to construct kinetic barrier diagrams is presented. Although the diagram superficially resembles a free-energy profile, it is independent of any conception derived from transition-state theory. Some simple calculations referring to the lactate dehydrogenase turnover reaction at equilibrium demonstrate self-consistency of the diagram and its direct relevance to the results of numerical simulations of the detailed course of enzyme-catalysed reactions.

摘要

本文提出了一种构建动力学势垒图的改进方法。尽管该图表面上类似于自由能曲线,但它独立于任何源自过渡态理论的概念。一些关于乳酸脱氢酶在平衡状态下周转反应的简单计算证明了该图的自洽性及其与酶催化反应详细过程数值模拟结果的直接相关性。