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猪心延胡索酸酶在恒定离子强度下确实表现出负动力学协同性。

Pig heart fumarase really does exhibit negative kinetic co-operativity at a constant ionic strength.

作者信息

Hasinoff B B, Davey J P

出版信息

Biochem J. 1986 May 1;235(3):891-3. doi: 10.1042/bj2350891.

DOI:10.1042/bj2350891
PMID:3753451
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1146771/
Abstract

The kinetics of the action of fumarase on L-malate and fumarate were investigated at constant ionic strength. This was done to evaluate reports that fumarase follows simple Michaelis-Menten kinetics. However, when pH, buffer concentration and ionic strength are all maintained at constant values, the Lineweaver-Burk plots exhibit pronounced downward curvature, characteristic of negative kinetic co-operativity.

摘要

在恒定离子强度下研究了延胡索酸酶作用于L-苹果酸和富马酸的动力学。这样做是为了评估有关延胡索酸酶遵循简单米氏动力学的报道。然而,当pH值、缓冲液浓度和离子强度都保持恒定时,Lineweaver-Burk图呈现出明显的向下弯曲,这是负动力学协同性的特征。

相似文献

1
Pig heart fumarase really does exhibit negative kinetic co-operativity at a constant ionic strength.猪心延胡索酸酶在恒定离子强度下确实表现出负动力学协同性。
Biochem J. 1986 May 1;235(3):891-3. doi: 10.1042/bj2350891.
2
Chicken fumarase. II. Kinetic studies.鸡延胡索酸酶。II. 动力学研究。
Biochimie. 1975;57(2):131-8. doi: 10.1016/s0300-9084(75)80162-3.
3
Lack of deviation from Michaelis--Menten kinetics for pig heart fumarase.猪心富马酸酶未偏离米氏动力学。
Biochem J. 1980 Sep 1;189(3):653-4. doi: 10.1042/bj1890653.
4
Evidence against a step-wise mechanism for the fumarase-catalysed dehydration of (2S)-malate.反对富马酸酶催化(2S)-苹果酸脱水的逐步机制的证据。
Eur J Biochem. 1980 Jul;108(2):433-7. doi: 10.1111/j.1432-1033.1980.tb04739.x.
5
Thermodynamics of the conversion of fumarate to L-(-)-malate.
Biophys Chem. 1985 Aug;22(3):187-95. doi: 10.1016/0301-4622(85)80042-9.
6
Sub-minute kinetics of human red cell fumarase: H spin-echo NMR spectroscopy and C rapid-dissolution dynamic nuclear polarization.人红细胞富马酸酶的亚分钟动力学:氢自旋回波核磁共振光谱法和碳快速溶解动态核极化
NMR Biomed. 2018 Mar;31(3). doi: 10.1002/nbm.3870. Epub 2018 Jan 8.
7
Kinetics of enzymes with iso-mechanisms: dead-end inhibition of fumarase and carbonic anhydrase II.具有同工机制的酶的动力学:延胡索酸酶和碳酸酐酶II的终产物抑制作用
Arch Biochem Biophys. 1994 Jul;312(1):227-33. doi: 10.1006/abbi.1994.1303.
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How fumarase recycles after the malate --> fumarate reaction. Insights into the reaction mechanism.苹果酸转化为富马酸反应后富马酸酶如何循环利用。对反应机制的见解。
Biochemistry. 1998 Dec 22;37(51):17651-8. doi: 10.1021/bi9821521.
9
[The effect of composition and ionic strength of external solution on the aspartate-ammonia lyase and fumarate hydratase activity in Escherichia coli cells].[外部溶液的组成和离子强度对大肠杆菌细胞中天冬氨酸氨裂解酶和富马酸水合酶活性的影响]
Biokhimiia. 1989 Dec;54(12):1994-9.
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A differential labelling model for determining the number of catalytically essential carboxyl groups in fumarase.一种用于确定延胡索酸酶中催化必需羧基数量的差异标记模型。
Biochim Biophys Acta. 1981 Dec 15;662(2):196-201. doi: 10.1016/0005-2744(81)90030-9.

引用本文的文献

1
Identification of the catalytic mechanism and estimation of kinetic parameters for fumarase.鉴定延胡索酸酶的催化机制并估算其动力学参数。
J Biol Chem. 2011 Jun 17;286(24):21100-9. doi: 10.1074/jbc.M110.214452. Epub 2011 Apr 15.

本文引用的文献

1
Alteration of the Kinetic Properties of an Enzyme by the Binding of Buffer, Inhibitor, or Substrate.缓冲液、抑制剂或底物的结合对酶动力学性质的改变。
Proc Natl Acad Sci U S A. 1953 Sep;39(9):895-900. doi: 10.1073/pnas.39.9.895.
2
Cooperativity in enzyme function: equilibrium and kinetic aspects.酶功能中的协同性:平衡和动力学方面
Methods Enzymol. 1980;64:139-92. doi: 10.1016/s0076-6879(80)64009-9.
3
Lack of deviation from Michaelis--Menten kinetics for pig heart fumarase.猪心富马酸酶未偏离米氏动力学。
Biochem J. 1980 Sep 1;189(3):653-4. doi: 10.1042/bj1890653.
4
Half-time analysis of the integrated Michaelis equation. Simulation and use of the half-time plot and its direct linear variant in the analysis of some alpha-chymotrypsin, papain- and fumarase-catalysed reactions.米氏积分方程的半衰期分析。半衰期图及其直接线性变体在某些α-糜蛋白酶、木瓜蛋白酶和延胡索酸酶催化反应分析中的模拟与应用。
Biochem J. 1982 May 1;203(2):351-60. doi: 10.1042/bj2030351.
5
Deviations from Michaelis-Menten kinetics. The possibility of complicated curves for simple kinetic schemes and the computer fitting of experimental data for acetylcholinesterase, acid phosphatase, adenosine deaminase, arylsulphatase, benzylamine oxidase, chymotrypsin, fumarase, galactose dehydrogenase, beta-galactosidase, lactate dehydrogenase, peroxidase and xanthine oxidase.与米氏动力学的偏差。简单动力学机制出现复杂曲线的可能性以及对乙酰胆碱酯酶、酸性磷酸酶、腺苷脱氨酶、芳基硫酸酯酶、苄胺氧化酶、胰凝乳蛋白酶、延胡索酸酶、半乳糖脱氢酶、β-半乳糖苷酶、乳酸脱氢酶、过氧化物酶和黄嘌呤氧化酶的实验数据进行计算机拟合。
Biochem J. 1980 Jun 1;187(3):739-65. doi: 10.1042/bj1870739.
6
Fumarase: demonstration, separation, and hybridization of different subunit types.
J Biol Chem. 1971 Jul 10;246(13):4261-5.
7
A new purification procedure for fumarase based of affinity chromatography. Isolation and characterization of pig-liver fumarase.
Eur J Biochem. 1977 Sep;78(2):437-44. doi: 10.1111/j.1432-1033.1977.tb11756.x.