天冬氨酸转氨甲酰酶协同性的动力学模型。

A kinetic model of cooperativity in aspartate transcarbamylase.

作者信息

Dembo M, Rubinow S I

出版信息

Biophys J. 1977 Jun;18(3):245-67. doi: 10.1016/S0006-3495(77)85611-7.

DOI:10.1016/S0006-3495(77)85611-7

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1473294/

Abstract

A relatively simple kinetic model is proposed to account simultaneously for data on the binding of carbamyl phosphate and succinate to aspartate trans carbamylase (ATCase), and for the relaxation spectrum associated with this binding. The model also accounts for measurements of the initial velocity of the reaction of ATCase with respect to aspartate and carbamyl phosphate. The principal assumption made is that ATCase consists of three identical noninteracting cooperative dimers. Ordered binding and both sequential and concerted conformational changes in the dimers are needed to account for the properties of ATCase. The values of the parameters of this model can be determined by fitting to existing experimental evidence. Various new quantitative predictions are made that can serve as additional tests of the proposed theory.

摘要

提出了一个相对简单的动力学模型，以同时解释氨甲酰磷酸和琥珀酸与天冬氨酸转氨甲酰酶（ATCase）结合的数据，以及与此结合相关的弛豫光谱。该模型还解释了ATCase与天冬氨酸和氨甲酰磷酸反应的初始速度的测量结果。所做的主要假设是，ATCase由三个相同的非相互作用的协同二聚体组成。需要有序结合以及二聚体中的顺序和协同构象变化来解释ATCase的特性。该模型参数的值可以通过拟合现有实验证据来确定。做出了各种新的定量预测，可作为对所提出理论的额外检验。

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本文引用的文献

1

ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.关于别构转变的本质：一个合理的模型。

J Mol Biol. 1965 May;12:88-118. doi: 10.1016/s0022-2836(65)80285-6.

2

The enzymology of control by feedback inhibition.反馈抑制控制的酶学

J Biol Chem. 1962 Mar;237:891-6.

3

Comparison of experimental binding data and theoretical models in proteins containing subunits.含亚基蛋白质中实验结合数据与理论模型的比较。

Biochemistry. 1966 Jan;5(1):365-85. doi: 10.1021/bi00865a047.

4

Crystallographic determination of symmetry of aspartate transcarbamylase.天冬氨酸转氨甲酰酶对称性的晶体学测定

Nature. 1968 Jun 22;218(5147):1119-21. doi: 10.1038/2181119a0.

5

Interpretation of nonhyperbolic behavior in enzymic systems. II. Quantitative characteristics of rate and binding functions.酶系统中非双曲线行为的解读。II. 速率和结合函数的定量特征。

Can J Biochem. 1971 May;49(5):581-98. doi: 10.1139/o71-085.

6

Conformational changes in proteins as measured by difference sedimentation studies. II. Effect of stereospecific ligands on the catalytic subunit of aspartate transcarbamylase.

Biochemistry. 1971 May 11;10(10):1919-26. doi: 10.1021/bi00786a028.

7

Conformational changes in proteins as measured by difference sedimentation studies. I. A technique for measuring small changes in sedimentation coefficient.

Biochemistry. 1971 May 11;10(10):1900-19. doi: 10.1021/bi00786a027.

8

Conformational changes in aspartate transcarbamylase. 3. A functional model for allosteric behavior.

J Biol Chem. 1971 Feb 10;246(3):762-71.

9

Determination of the number of regulatory and catalytic sites on aspartate transcarbamylase.

Biochemistry. 1970 Jul 21;9(15):2992-4. doi: 10.1021/bi00817a009.

10

Distinct subunits for the regulation and catalytic activity of aspartate transcarbamylase.天冬氨酸转氨甲酰酶调节和催化活性的不同亚基。

Biochemistry. 1965 Jun;4(6):1054-62. doi: 10.1021/bi00882a012.

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