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1
A steady-state random-order mechanism for the oxidative deamination of norvaline by glutamate dehydrogenase.谷氨酸脱氢酶催化正缬氨酸氧化脱氨的稳态随机顺序机制。
Biochem J. 1983 Apr 1;211(1):99-107. doi: 10.1042/bj2110099.
2
A product-inhibition study of bovine liver glutamate dehydrogenase.牛肝谷氨酸脱氢酶的产物抑制研究。
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3
The kinetic mechanism of ox liver glutamate dehydrogenase in the presence of the allosteric effector ADP. The oxidative deamination of L-glutamate.变构效应物ADP存在时牛肝谷氨酸脱氢酶的动力学机制。L-谷氨酸的氧化脱氨作用。
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4
Kinetic studies of glutamate dehydrogenase. The reductive amination of 2-oxoglutarate.谷氨酸脱氢酶的动力学研究。2-氧代戊二酸的还原胺化作用。
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5
Kinetic studies of dogfish liver glutamate dehydrogenase.角鲨肝脏谷氨酸脱氢酶的动力学研究。
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6
Kinetic studies of glutamate dehydrogenase with glutamate and norvaline as substrates. Coenzyme activation and negative homotropic interactions in allosteric enzymes.以谷氨酸和正缬氨酸为底物的谷氨酸脱氢酶动力学研究。变构酶中的辅酶激活和负协同相互作用。
Biochem J. 1969 Dec;115(4):621-31. doi: 10.1042/bj1150621.
7
Equilibrium kinetic study of the catalytic mechanism of oxidative deamination of alanine by bovine liver glutamate dehydrogenase.牛肝谷氨酸脱氢酶催化丙氨酸氧化脱氨反应机制的平衡动力学研究
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8
Nickel-induced substrate inhibition of bovine liver glutamate dehydrogenase.镍诱导的牛肝谷氨酸脱氢酶底物抑制作用。
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A kinetic study of the oxidative deamination of L-glutamate by Peptostreptococcus asaccharolyticus glutamate dehydrogenase using a variety of coenzymes.利用多种辅酶对解糖消化链球菌谷氨酸脱氢酶催化L-谷氨酸氧化脱氨作用的动力学研究。
Eur J Biochem. 1984 Sep 17;143(3):557-60. doi: 10.1111/j.1432-1033.1984.tb08405.x.
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Negative co-operativity in glutamate dehydrogenase. Involvement of the 2-position in glutamate in the induction of conformational changes.谷氨酸脱氢酶中的负协同性。谷氨酸2位在构象变化诱导中的作用。
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引用本文的文献

1
Multiple Forms of Glutamate Dehydrogenase in Animals: Structural Determinants and Physiological Implications.动物体内谷氨酸脱氢酶的多种形式：结构决定因素及生理意义
Biology (Basel). 2016 Dec 14;5(4):53. doi: 10.3390/biology5040053.
2
A novel mechanism of V-type zinc inhibition of glutamate dehydrogenase results from disruption of subunit interactions necessary for efficient catalysis.一种新型的 V 型锌抑制谷氨酸脱氢酶的机制源于破坏了有效催化所必需的亚基相互作用。
FEBS J. 2011 Sep;278(17):3140-51. doi: 10.1111/j.1742-4658.2011.08240.x. Epub 2011 Aug 11.
3
Ligand-induced changes in the conformational stability and flexibility of glutamate dehydrogenase and their role in catalysis and regulation.配体诱导谷氨酸脱氢酶构象稳定性和灵活性的变化及其在催化和调节中的作用。
Protein Sci. 2010 Oct;19(10):1820-9. doi: 10.1002/pro.459.
4
Negative co-operativity in glutamate dehydrogenase. Involvement of the 2-position in glutamate in the induction of conformational changes.谷氨酸脱氢酶中的负协同性。谷氨酸2位在构象变化诱导中的作用。
Biochem J. 1985 Jan 1;225(1):209-17. doi: 10.1042/bj2250209.

本文引用的文献

1
The substrate specificity of glutamic acid dehydrogenase.谷氨酸脱氢酶的底物特异性。
Arch Biochem Biophys. 1960 Feb;86:260-6. doi: 10.1016/0003-9861(60)90415-x.
2
Glutamic dehydrogenase. III. The order of substrate addition in the enzymatic reaction.谷氨酸脱氢酶。III. 酶促反应中底物添加的顺序。
J Biol Chem. 1959 Nov;234:2891-6.
3
The mechanism of the glutamic dehydrogenase reaction. I. The molecularity of the first complex formed.谷氨酸脱氢酶反应的机制。I. 所形成的第一个复合物的分子数。
J Biol Chem. 1960 Jun;235:1830-4.
4
Dual nucleotide specificity of bovine glutamate dehydrogenase. The role of negative co-operativity.牛谷氨酸脱氢酶的双核苷酸特异性。负协同效应的作用。
Biochem J. 1980 Nov 1;191(2):299-304. doi: 10.1042/bj1910299.
5
Kinetic mechanism of glutamate dehydrogenase.谷氨酸脱氢酶的动力学机制。
Biochemistry. 1980 May 27;19(11):2321-8. doi: 10.1021/bi00552a007.
6
Regulation of bovine glutamate dehydrogenase. The effects of pH and ADP.牛谷氨酸脱氢酶的调节。pH值和二磷酸腺苷的影响。
J Biol Chem. 1982 May 25;257(10):5579-83.
7
[Regulation of the activity of glutamate dehydrogenase by effectors GTP and ADP: study by means of "stopped flow"].[效应物GTP和ADP对谷氨酸脱氢酶活性的调节：采用“停流法”的研究]
Bull Soc Chim Biol (Paris). 1967 Dec 18;49(11):1563-72.
8
Spectrophotometric observation of a glutamate dehydrogenase-L-glutamate complex.谷氨酸脱氢酶-L-谷氨酸复合物的分光光度观察
Biochim Biophys Acta. 1972 Sep 19;284(1):16-9. doi: 10.1016/0005-2744(72)90040-x.
9
The mechanism of glutamate dehydrogenase reaction. IV. Evidence for random and rapid binding of substrate and coenzyme in the burst phase.谷氨酸脱氢酶反应的机制。IV。在反应起始阶段底物和辅酶随机且快速结合的证据。
J Biol Chem. 1972 Dec 25;247(24):7905-9.
10
Reaction mechanism of L-glutamate dehydrogenase. Characterization of optical and kinetic properties of various enzyme-reduced-coenzyme complexes.L-谷氨酸脱氢酶的反应机制。各种酶-还原辅酶复合物的光学和动力学性质表征。
Eur J Biochem. 1972 Nov 7;30(3):517-32. doi: 10.1111/j.1432-1033.1972.tb02123.x.

谷氨酸脱氢酶催化正缬氨酸氧化脱氨的稳态随机顺序机制。

A steady-state random-order mechanism for the oxidative deamination of norvaline by glutamate dehydrogenase.

作者信息

LiMuti C, Bell J E

出版信息

Biochem J. 1983 Apr 1;211(1):99-107. doi: 10.1042/bj2110099.

DOI:10.1042/bj2110099
PMID:6870833
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1154333/
Abstract

The kinetic mechanism of glutamate dehydrogenase with the monocarboxylic substrate norvaline was examined by using initial-rate steady-state kinetics and inhibition kinetics. To a first approximation the reaction mechanism can be described as a rapid-equilibrium random-order one. Binding synergism between the monocarboxylic substrate and coenzyme is not observed. Dissociation constants for NAD+ and 2-oxoglutarate calculated from the kinetic data assuming a rapid-equilibrium random-order model are in good agreement with independently obtained estimates. Lineweaver-Burk plots with varied norvaline concentration are not strictly linear, and it is concluded that a steady-state random-order model more accurately reflects the observed kinetics with norvaline as substrate.

摘要

通过使用初速率稳态动力学和抑制动力学，研究了谷氨酸脱氢酶与单羧酸底物正缬氨酸的动力学机制。初步估算，该反应机制可描述为快速平衡随机顺序机制。未观察到单羧酸底物与辅酶之间的结合协同作用。根据动力学数据，假设为快速平衡随机顺序模型计算得到的NAD⁺和2-氧代戊二酸的解离常数，与独立获得的估计值高度吻合。以不同正缬氨酸浓度绘制的林-贝氏图并非严格呈线性，由此得出结论，稳态随机顺序模型能更准确地反映以正缬氨酸为底物时所观察到的动力学。