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Kinetic parameters of the acyl-enzyme mechanism and conditions for quasi-equilibrium and for optimal catalytic characteristics.酰基酶机制的动力学参数以及准平衡和最佳催化特性的条件。
Biochem J. 1990 Sep 1;270(2):561-3. doi: 10.1042/bj2700561.
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Kinetic analysis of a Michaelis-Menten mechanism in which the enzyme is unstable.对一种酶不稳定的米氏(Michaelis-Menten)机制的动力学分析。
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Evolution of enzyme catalytic power. Characteristics of optimal catalysis evaluated for the simplest plausible kinetic model.酶催化能力的演变。针对最简单合理动力学模型评估的最佳催化特性。
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Beta-secondary and solvent deuterium kinetic isotope effects on catalysis by the Streptomyces R61 DD-peptidase: comparisons with a structurally similar class C beta-lactamase.链霉菌R61 DD-肽酶催化作用的β-二级和溶剂氘动力学同位素效应:与结构相似的C类β-内酰胺酶的比较。
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Mechanistic studies of carboxypeptidase Y. Kinetic detection of an acyl-enzyme intermediate in trimethylacetate esterase action.
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Catalysis, binding and enzyme-substrate complementarity.催化、结合与酶-底物互补性。
Proc R Soc Lond B Biol Sci. 1974 Nov 19;187(1089):397-407. doi: 10.1098/rspb.1974.0084.

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Theoretical Improvements in Enzyme Efficiency Associated with Noisy Rate Constants and Increased Dissipation.与噪声速率常数和增加的耗散相关的酶效率的理论改进。
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Preparation and characterization of a truncated caricain lacking 41 residues from the N-terminal.一种从N端缺失41个残基的截短型木瓜蛋白酶的制备与表征。
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Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine.莽草酸激酶的生化及X射线晶体学研究:P环赖氨酸的重要结构作用
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Efficient catalysis by beta-lactamase from Staphylococcus aureus PC1 accompanied by accumulation of an acyl-enzyme.金黄色葡萄球菌PC1的β-内酰胺酶的高效催化作用伴随着酰基酶的积累。
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Some classical errors in the kinetic analysis of enzyme reactions.酶反应动力学分析中的一些经典错误。
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Site-directed mutagenesis of beta-lactamase I. Single and double mutants of Glu-166 and Lys-73.β-内酰胺酶I的定点诱变。Glu-166和Lys-73的单突变体和双突变体。
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Structure-function relationships in the cysteine proteinases actinidin, papain and papaya proteinase omega. Three-dimensional structure of papaya proteinase omega deduced by knowledge-based modelling and active-centre characteristics determined by two-hydronic-state reactivity probe kinetics and kinetics of catalysis.半胱氨酸蛋白酶肌动蛋白水解酶、木瓜蛋白酶和木瓜蛋白酶ω的结构-功能关系。通过基于知识的建模推导木瓜蛋白酶ω的三维结构,以及通过双水合态反应探针动力学和催化动力学确定其活性中心特征。
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本文引用的文献

1
THE inhibition of chymotrypsin by diethyl p-nitrophenyl phosphate.对硝基苯基磷酸二乙酯对胰凝乳蛋白酶的抑制作用。
Biochem J. 1952 Mar;50(5):672-8. doi: 10.1042/bj0500672.
2
MECHANISM OF ACTION OF PROTEOLYTIC ENZYMES.蛋白水解酶的作用机制
Annu Rev Biochem. 1965;34:49-76. doi: 10.1146/annurev.bi.34.070165.000405.
3
The mechanism of the reaction of chymotrypsin with p-nitrophenyl acetate.胰凝乳蛋白酶与对硝基苯乙酸反应的机制。
Biochem J. 1956 Aug;63(4):656-61. doi: 10.1042/bj0630656.
4
The reaction of p-nitrophenyl esters with chymotrypsin and insulin.对硝基苯酯与胰凝乳蛋白酶和胰岛素的反应。
Biochem J. 1954 Feb;56(2):288-97. doi: 10.1042/bj0560288.
5
The kinetic analysis of hydrolytic enzyme catalyses: Consequences of non-productive binding.水解酶催化的动力学分析:非生产性结合的后果。
FEBS Lett. 1968 Nov;2(1):69-73. doi: 10.1016/0014-5793(68)80103-6.
6
Triosephosphate isomerase catalysis is diffusion controlled. Appendix: Analysis of triose phosphate equilibria in aqueous solution by 31P NMR.磷酸丙糖异构酶催化作用受扩散控制。附录:通过³¹P NMR分析水溶液中的磷酸丙糖平衡。
Biochemistry. 1988 Feb 23;27(4):1158-67. doi: 10.1021/bi00404a013.
7
Accumulation of acyl-enzyme intermediates during turnover of penicillins by the class A beta-lactamase of Staphylococcus aureus PC1.金黄色葡萄球菌PC1的A类β-内酰胺酶在青霉素周转过程中酰基酶中间体的积累。
Biochem J. 1988 Sep 15;254(3):919-22. doi: 10.1042/bj2540919.
8
Effect of evolution on the kinetic properties of enzymes.进化对酶动力学性质的影响。
Eur J Biochem. 1989 Oct 1;184(3):561-6. doi: 10.1111/j.1432-1033.1989.tb15050.x.
9
Trypsin-like serine proteinase action: determination of the catalytic parameters KS, k+2 and k/3 under conditions where the substrate exceeds the enzyme concentration.类胰蛋白酶丝氨酸蛋白酶活性:在底物浓度超过酶浓度的条件下测定催化参数KS、k+2和k/3。
Biochim Biophys Acta. 1989 Oct 5;998(2):210-4. doi: 10.1016/0167-4838(89)90275-6.
10
Internal thermodynamics of enzymes determined by equilibrium quench: values of Kint for enolase and creatine kinase.通过平衡淬灭法测定的酶的内部热力学:烯醇化酶和肌酸激酶的Kint值
Biochemistry. 1989 Nov 28;28(24):9306-17. doi: 10.1021/bi00450a010.

Kinetic parameters of the acyl-enzyme mechanism and conditions for quasi-equilibrium and for optimal catalytic characteristics.

作者信息

Brocklehurst K, Topham C M

机构信息

Department of Biochemistry, Medical College of St. Bartholomew's Hospital, University of London, U.K.

出版信息

Biochem J. 1990 Sep 1;270(2):561-3. doi: 10.1042/bj2700561.

DOI:10.1042/bj2700561
PMID:2400403
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1131762/
Abstract
摘要