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A steady-state-kinetic random mechanism for glutathione S-transferase A from rat liver. A model involving kinetically significant enzyme-product complexes in the forward reaction.

作者信息

Jakobson I, Askelöf P, Warholm M, Mannervik B

出版信息

Eur J Biochem. 1977 Jul 15;77(2):253-62. doi: 10.1111/j.1432-1033.1977.tb11664.x.

DOI:10.1111/j.1432-1033.1977.tb11664.x
PMID:891533
Abstract
摘要

相似文献

1
A steady-state-kinetic random mechanism for glutathione S-transferase A from rat liver. A model involving kinetically significant enzyme-product complexes in the forward reaction.大鼠肝脏谷胱甘肽S-转移酶A的稳态动力学随机机制。一种在前向反应中涉及具有动力学意义的酶-产物复合物的模型。
Eur J Biochem. 1977 Jul 15;77(2):253-62. doi: 10.1111/j.1432-1033.1977.tb11664.x.
2
The binding of substrates and a product of the enzymatic reaction to glutathione S-transferase A.
J Biol Chem. 1979 Aug 10;254(15):7085-9.
3
Multiple inhibition of glutathione S-transferase A from rat liver by glutathione derivatives: kinetic analysis supporting a steady-state random sequential mechanism.谷胱甘肽衍生物对大鼠肝脏谷胱甘肽S-转移酶A的多重抑制作用：支持稳态随机顺序机制的动力学分析
Biochem J. 1979 Mar 1;177(3):861-8. doi: 10.1042/bj1770861.
4
Kinetic independence of the subunits of cytosolic glutathione transferase from the rat.大鼠胞质谷胱甘肽转移酶亚基的动力学独立性
Biochem J. 1985 Oct 15;231(2):263-7. doi: 10.1042/bj2310263.
5
Explanation of the non-hyperbolic kinetics of the glutathione S-transferases by the simplest steady-state random sequential Bi Bi mechanism.通过最简单的稳态随机顺序双底物双产物机制对谷胱甘肽S-转移酶的非双曲线动力学进行解释。
Biochem Pharmacol. 1990 Jun 15;39(12):1999-2004. doi: 10.1016/0006-2952(90)90621-q.
6
Absence of a ping-pong pathway in the kinetic mechanism of glutathione S-transferase A from rat liver. Evidence based on quantitative comparison of the asymptotic properties of experimental data and alternative rat equations.大鼠肝脏谷胱甘肽S-转移酶A动力学机制中乒乓途径的缺失。基于实验数据渐近性质与替代大鼠方程定量比较的证据。
FEBS Lett. 1975 Aug 15;56(2):218-21. doi: 10.1016/0014-5793(75)81095-7.
7
Steady-state kinetics and chemical mechanism of octopus hepatopancreatic glutathione transferase.章鱼肝胰腺谷胱甘肽转移酶的稳态动力学和化学机制
Biochem J. 1995 Jul 1;309 ( Pt 1)(Pt 1):347-53. doi: 10.1042/bj3090347.
8
The effect of ethanol on the steady-state kinetics of glutathione S-transferase A from rat liver.乙醇对大鼠肝脏谷胱甘肽S-转移酶A稳态动力学的影响。
FEBS Lett. 1979 Jun 1;102(1):165-8. doi: 10.1016/0014-5793(79)80951-5.
9
Kinetic analysis of the slow ionization of glutathione by microsomal glutathione transferase MGST1.微粒体谷胱甘肽转移酶MGST1催化谷胱甘肽缓慢电离的动力学分析。
Biochemistry. 2001 Mar 20;40(11):3378-84. doi: 10.1021/bi0023394.
10
Fast product formation and slow product release are important features in a hysteretic reaction mechanism of glutathione transferase T2-2.快速的产物形成和缓慢的产物释放是谷胱甘肽转移酶T2-2滞后反应机制的重要特征。
Biochemistry. 1999 Aug 3;38(31):9982-91. doi: 10.1021/bi983065b.

引用本文的文献

1
Kinetic Behavior of Glutathione Transferases: Understanding Cellular Protection from Reactive Intermediates.谷胱甘肽转移酶的动力学行为：理解细胞对反应中间体的保护作用。
Biomolecules. 2024 May 30;14(6):641. doi: 10.3390/biom14060641.
2
Repurposing Glutathione Transferases: Directed Evolution Combined with Chemical Modification for the Creation of a Semisynthetic Enzyme with High Hydroperoxidase Activity.谷胱甘肽转移酶的功能拓展：通过定向进化与化学修饰构建具有高氢过氧化物酶活性的半合成酶
Antioxidants (Basel). 2023 Dec 25;13(1):41. doi: 10.3390/antiox13010041.
3
Global Kinetic Mechanism of Microsomal Glutathione Transferase 1 and Insights into Dynamic Enzyme Activation.
微粒体谷胱甘肽转移酶1的全局动力学机制及对动态酶激活的见解
Biochemistry. 2017 Jun 20;56(24):3089-3098. doi: 10.1021/acs.biochem.7b00285. Epub 2017 Jun 9.
4
Purification and characterization of three forms of glutathione S-transferase A. A comparative study of the major YaYa-, YbYb- and YcYc-containing glutathione S-transferases.三种形式谷胱甘肽S-转移酶A的纯化与特性分析。含主要YaYa-、YbYb-和YcYc-的谷胱甘肽S-转移酶的比较研究。
Biochem J. 1982 Dec 1;207(3):459-70. doi: 10.1042/bj2070459.
5
Purification and characterization of glutathione S-transferases P, S and N. Isolation from rat liver of Yb1 Yn protein, the existence of which was predicted by subunit hybridization in vitro.谷胱甘肽S-转移酶P、S和N的纯化与特性分析。从大鼠肝脏中分离出Yb1 Yn蛋白，其存在是通过体外亚基杂交预测的。
Biochem J. 1984 Dec 15;224(3):839-52. doi: 10.1042/bj2240839.
6
Kinetic independence of the subunits of cytosolic glutathione transferase from the rat.大鼠胞质谷胱甘肽转移酶亚基的动力学独立性
Biochem J. 1985 Oct 15;231(2):263-7. doi: 10.1042/bj2310263.
7
Inhibition of hepatic and extrahepatic glutathione S-transferases by primary and secondary bile acids.初级和次级胆汁酸对肝脏和肝外谷胱甘肽S-转移酶的抑制作用。
Biochem J. 1986 Jan 15;233(2):407-15. doi: 10.1042/bj2330407.
8
Error structure as a function of substrate and inhibitor concentration in enzyme kinetic experiments.酶动力学实验中作为底物和抑制剂浓度函数的误差结构
Biochem J. 1986 May 1;235(3):797-804. doi: 10.1042/bj2350797.
9
Paradoxical inhibition of rat glutathione transferase 4-4 by indomethacin explained by substrate-inhibitor-enzyme complexes in a random-order sequential mechanism.吲哚美辛对大鼠谷胱甘肽转移酶4-4的反常抑制作用，由随机顺序序列机制中的底物-抑制剂-酶复合物解释。
Biochem J. 1988 Mar 15;250(3):705-11. doi: 10.1042/bj2500705.
10
Purification and kinetic mechanism of the major glutathione S-transferase from bovine brain.牛脑主要谷胱甘肽S-转移酶的纯化及动力学机制
Biochem J. 1989 Jan 15;257(2):541-8. doi: 10.1042/bj2570541.