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Haldane-Radić 酶动力学对传统和逻辑斯谛 Michaelis-Menten 模型的可约性。

On the reducible character of Haldane-Radić enzyme kinetics to conventional and logistic Michaelis-Menten models.

机构信息

Laboratory of Computational and Structural Physical Chemistry, Chemistry Department, West University of Timişoara, Pestalozzi Street No.16, Timisoara, RO-300115, Romania.

出版信息

Molecules. 2011 Apr 13;16(4):3128-45. doi: 10.3390/molecules16043128.

DOI:10.3390/molecules16043128
PMID:21490560
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6260611/
Abstract

The conceptual and practical issues regarding the reduction of the Haldane-Radić enzymic mechanism, specific for cholinesterase kinetics, to the consecrated or logistically modified Michaelis-Menten kinetics, specific for some mutant enzymes, are here clarified as due to the limited initial substrate concentration, through detailed initial rate and progress curve analysis, even when other classical conditions for such equivalence are not entirely fulfilled.

摘要

有关将特定于胆碱酯酶动力学的 Haldane-Radić 酶促机制简化为特定于某些突变酶的传统或逻辑修改的 Michaelis-Menten 动力学的概念和实际问题，通过详细的初始速率和进展曲线分析，即使其他经典等效条件不完全满足，也可以阐明这些问题是由于初始底物浓度有限所致。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/666f/6260611/818b8952b3ce/molecules-16-03128-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/666f/6260611/f1cd92bc618c/molecules-16-03128-g007.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/666f/6260611/1621fae42419/molecules-16-03128-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/666f/6260611/f3592f044aa9/molecules-16-03128-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/666f/6260611/bd792ada36d4/molecules-16-03128-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/666f/6260611/4b00dab875c6/molecules-16-03128-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/666f/6260611/818b8952b3ce/molecules-16-03128-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/666f/6260611/f1cd92bc618c/molecules-16-03128-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/666f/6260611/35a10dcfe36c/molecules-16-03128-g008.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/666f/6260611/f3592f044aa9/molecules-16-03128-g003.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/666f/6260611/4b00dab875c6/molecules-16-03128-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/666f/6260611/818b8952b3ce/molecules-16-03128-g006.jpg

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本文引用的文献

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Insights into substrate and product traffic in the Drosophila melanogaster acetylcholinesterase active site gorge by enlarging a back channel.通过扩大一条后通道深入了解黑腹果蝇乙酰胆碱酯酶活性位点峡谷中的底物和产物运输情况。
FEBS J. 2008 May;275(10):2659-64. doi: 10.1111/j.1742-4658.2008.06413.x. Epub 2008 Apr 15.
2
Determination of complex reaction mechanisms. Analysis of chemical, biological and genetic networks.复杂反应机制的确定。化学、生物和遗传网络分析。
J Phys Chem A. 2008 Mar 20;112(11):2134-43. doi: 10.1021/jp711313e. Epub 2008 Feb 15.
3
Probing the mechanism of the bifunctional enzyme ketol-acid reductoisomerase by site-directed mutagenesis of the active site.
通过对活性位点进行定点诱变来探究双功能酶酮醇酸还原异构酶的作用机制。
FEBS J. 2005 Jan;272(2):593-602. doi: 10.1111/j.1742-4658.2004.04506.x.
4
Progress curve analysis for enzyme and microbial kinetic reactions using explicit solutions based on the Lambert W function.基于兰伯特W函数显式解的酶促和微生物动力学反应的进展曲线分析。
J Microbiol Methods. 2004 Dec;59(3):317-26. doi: 10.1016/j.mimet.2004.06.013.
5
Inhibition of Drosophila melanogaster acetylcholinesterase by high concentrations of substrate.高浓度底物对黑腹果蝇乙酰胆碱酯酶的抑制作用。
Eur J Biochem. 2004 Apr;271(7):1364-71. doi: 10.1111/j.1432-1033.2004.04048.x.
6
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.
7
Parameter estimation using a direct solution of the integrated Michaelis-Menten equation.使用米氏方程积分的直接解进行参数估计。
Biochim Biophys Acta. 1999 Jan 11;1429(2):377-83. doi: 10.1016/s0167-4838(98)00247-7.
8
A putative kinetic model for substrate metabolisation by Drosophila acetylcholinesterase.
FEBS Lett. 1998 Nov 27;440(1-2):85-8. doi: 10.1016/s0014-5793(98)01434-3.
9
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors.胆碱酯酶分子中的三个不同结构域赋予了对乙酰胆碱酯酶和丁酰胆碱酯酶抑制剂的选择性。
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10
A new library of alpha-lytic protease S1 mutants generated by combinatorial random substitution.通过组合随机取代产生的α-溶胞素蛋白酶S1突变体新文库。
Biochem Mol Biol Int. 1994 Apr;32(5):831-9.