MECHANISM OF ALLOSTERIC INFLUENCE ON ENZYME ACTIVITY

变构对酶活性的影响机制

基本信息

  • 批准号:
    3282625
  • 负责人:
  • 金额:
    $ 18.38万
  • 依托单位:
  • 依托单位国家:
    美国
  • 项目类别:
  • 财政年份:
    1983
  • 资助国家:
    美国
  • 起止时间:
    1983-08-01 至 1994-06-30
  • 项目状态:
    已结题

项目摘要

A regulatory motif of fundamental importance to metabolic control is the allosteric modification of enzymatic activity. The long term objective of this application is to increase our understanding of the mechanisms by which allosteric ligands are able to modify enzymatic activity through binding to sites on the enzyme removed from the active site. In particular we are interested in systems in which the allosteric ligands achieve their effects by altering the affinity of enzyme for its substrate. We specifically propose to study three different allosteric systems: prokaryotic phosphofructokinase (PFK) isolated from both Escherichia coli and Bacillus stearothermophilus; carbamoyl phosphate synthetase (CPS) from E. Coli; and NAD-dependent isocitrate dehydrogenase (ICDH) obtained from beef heart mitochondria. All of these enzymes fulfill important regulatory niches in metabolism. Even more importantly for the objectives of this application, however, they present opportunities for answering mechanistic questions that have general relevance to many other allosteric enzymes. By studying these enzymes we hope to be able to answer several questions regarding allosteric response including the following: 1) Is it appropriate to view allosteric behavior in terms of a two-state model even when two X-ray crystal structures are known? 2) Can temperature alter the nature as well as the magnitude of allosteric response? 3) How can two structurally similar ligands have opposite allosteric effects when binding to the same site? and 4) Can a single quantitative model be derived to explain the actions of an allosteric ligand that achieves its effects by altering both the tertiary conformation and the aggregation state of an enzyme? Our approach begins with a systematic and thorough linked-function characterization of the actions of an allosteric ligand. This analysis yields terms that quantify not only the affinity of the substrate and effector ligand, but also the nature and magnitude of the allosteric influence. By monitoring the changes induced in these parameters by modifications of an experimental variable; such as ligand structure, enzyme structure, temperature, enzyme concentration, etc.; insight can be gained into the relationship between the experimental variable and the actions of the allosteric ligand. This approach will be complemented by physical studies; notably fluorescence intensity, spectral distribution, polarization, and lifetime measurements of intrinsic tryptophan residues and covalently attached extrinsic fluorescent probes; to further define the structural consequences resulting from allosteric ligand binding.
一个对代谢控制具有根本重要性的调控基序是

项目成果

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GREGORY Duncan REINHART其他文献

GREGORY Duncan REINHART的其他文献

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{{ truncateString('GREGORY Duncan REINHART', 18)}}的其他基金

2012/2013 Enzymes, Coenzymes, and Metabolic Pathways Gordon Research Conference
2012/2013 酶、辅酶和代谢途径戈登研究会议
  • 批准号:
    8510670
  • 财政年份:
    2012
  • 资助金额:
    $ 18.38万
  • 项目类别:
2012/2013 Enzymes, Coenzymes, and Metabolic Pathways Gordon Research Conference
2012/2013 酶、辅酶和代谢途径戈登研究会议
  • 批准号:
    8389080
  • 财政年份:
    2012
  • 资助金额:
    $ 18.38万
  • 项目类别:
Graduate Training in Molecular Biophysics
分子生物物理学研究生培训
  • 批准号:
    7089867
  • 财政年份:
    2003
  • 资助金额:
    $ 18.38万
  • 项目类别:
Graduate Training in Molecular Biophysics
分子生物物理学研究生培训
  • 批准号:
    7256505
  • 财政年份:
    2003
  • 资助金额:
    $ 18.38万
  • 项目类别:
MECHANISMS ON ALLOSTERIC INFLUENCES ON ENZYMES ACTIVITY
变构对酶活性影响的机制
  • 批准号:
    6385525
  • 财政年份:
    1983
  • 资助金额:
    $ 18.38万
  • 项目类别:
MECHANISM OF ALLOSTERIC INFLUENCE ON ENZYME ACTIVITY
变构对酶活性的影响机制
  • 批准号:
    3282618
  • 财政年份:
    1983
  • 资助金额:
    $ 18.38万
  • 项目类别:
Mechanisms of Allosteric Influence on Enzymes Activity
变构对酶活性的影响机制
  • 批准号:
    7743458
  • 财政年份:
    1983
  • 资助金额:
    $ 18.38万
  • 项目类别:
Mechanisms of Allosteric Influence on Enzymes Activity
变构对酶活性的影响机制
  • 批准号:
    8197459
  • 财政年份:
    1983
  • 资助金额:
    $ 18.38万
  • 项目类别:
MECHANISM OF ALLOSTERIC INFLUENCE ON ENZYME ACTIVITY
变构对酶活性的影响机制
  • 批准号:
    2176915
  • 财政年份:
    1983
  • 资助金额:
    $ 18.38万
  • 项目类别:
Mechanisms of Allosteric Influence on Enzymes Activity
变构对酶活性的影响机制
  • 批准号:
    7994240
  • 财政年份:
    1983
  • 资助金额:
    $ 18.38万
  • 项目类别:

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用于 DASL 等温扩增的重组改良嗜热脂肪芽孢杆菌 DNA 聚合酶的生产
  • 批准号:
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  • 批准号:
    6972674
  • 财政年份:
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  • 资助金额:
    $ 18.38万
  • 项目类别:
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  • 批准号:
    9713644
  • 财政年份:
    1997
  • 资助金额:
    $ 18.38万
  • 项目类别:
    Standard Grant
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温度依赖性质粒整合到嗜热脂肪芽孢杆菌染色体中以及从染色体中切除
  • 批准号:
    61470118
  • 财政年份:
    1986
  • 资助金额:
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  • 项目类别:
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