MOLECULAR PROPERTIES OF PEP CARBOXYLASE REVELANT TO ITS ALLOSTERIC REGULATION

PEP羧化酶的分子特性与其变构调节相关

基本信息

项目摘要

Phosphoenolpyruvate (PEP) carboxylase is of interest because of its central role in the photosynthetic metabolism of CAM and C4 plants. As would be expected for a key enzyme in a major metabolic pathway, the activity of the enzyme is highly regulated, and a fundamental regulatory element appears to be the interplay of the activation caused by phosphorylated activators such as glucose 6-phosphate and AMP and the inhibition caused by malate and ATP. The overall goal of this research is to elucidate various molecular aspects of the process by which effectors, particularly activators such as AMP and glucose 6-phosphate, regulate PEP carboxylase from Crassula argentea and other sources. The research will probe the binding site(s) of activators and inhibitors through the use of photoaffinity labels. The proposed research will also test the molecular mechanism of activation, in light of a novel hypothesis that has recently been proposed. The specific aims include estimating the number of activator binding sites and the dissociation constants for the activators, determining whether all activators share a common binding site, comparing the AMP and ATP binding sites, identifying the peptide sequence at the activator binding site, and testing the role of activator dephosphorylation in the activation process. The results are expected to provide molecular information on how and where activators exert their influence on the enzyme. This information will provide greater insight into the structure-function relationships of this specific enzyme and, more generally, into the process of metabolic regulation at the enzyme level.
磷酸烯醇丙酮酸(PEP)羧化酶之所以引起人们的兴趣,是因为它的中心

项目成果

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SCOTT D GROVER其他文献

SCOTT D GROVER的其他文献

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{{ truncateString('SCOTT D GROVER', 18)}}的其他基金

STRUCTURE/REGULATION RELATIONSHIPS IN PEP CARBOXYLASE
PEP 羧化酶的结构/调控关系
  • 批准号:
    6481216
  • 财政年份:
    2001
  • 资助金额:
    --
  • 项目类别:
STRUCTURE/REGULATION RELATIONSHIPS IN PEP CARBOXYLASE
PEP 羧化酶的结构/调控关系
  • 批准号:
    6325836
  • 财政年份:
    2000
  • 资助金额:
    --
  • 项目类别:
EFFECTOR BINDING SITES AND REGULATORY MECHNISIMS IN PEP CARBOXYLASE
PEP 羧化酶中的效应子结合位点和调控机制
  • 批准号:
    6107119
  • 财政年份:
    1999
  • 资助金额:
    --
  • 项目类别:
EFFECTOR BINDING SITES AND REGULATORY MECHNISIMS IN PEP CARBOXYLASE
PEP 羧化酶中的效应子结合位点和调控机制
  • 批准号:
    6296632
  • 财政年份:
    1998
  • 资助金额:
    --
  • 项目类别:
EFFECTOR BINDING SITES AND REGULATORY MECHNISIMS IN PEP CARBOXYLASE
PEP 羧化酶中的效应子结合位点和调控机制
  • 批准号:
    6271532
  • 财政年份:
    1998
  • 资助金额:
    --
  • 项目类别:
EFFECTOR BINDING SITES AND REGULATORY MECHNISIMS IN PEP CARBOXYLASE
PEP 羧化酶中的效应子结合位点和调控机制
  • 批准号:
    6240010
  • 财政年份:
    1997
  • 资助金额:
    --
  • 项目类别:
MOLECULAR PROPERTIES OF PEP CARBOXYLASE REVELANT TO ITS ALLOSTERIC REGULATION
PEP羧化酶的分子特性与其变构调节相关
  • 批准号:
    3734247
  • 财政年份:
  • 资助金额:
    --
  • 项目类别:
ENZYME HYSTERESIS AND AGGREGATION IN PEP CARBOXYLASE
PEP 羧化酶中的酶滞后和聚集
  • 批准号:
    3959458
  • 财政年份:
  • 资助金额:
    --
  • 项目类别:
EFFECT OF REGULATORY LIGANDS AND THEIR BINDING SITES ON PEP CARBOXYLASES
调节配体及其结合位点对 PEP 羧化酶的影响
  • 批准号:
    3915698
  • 财政年份:
  • 资助金额:
    --
  • 项目类别:
EFFECT OF REGULATORY LIGANDS AND THEIR BINDING SITES ON PEP CARBOXYLASES
调节配体及其结合位点对 PEP 羧化酶的影响
  • 批准号:
    3936807
  • 财政年份:
  • 资助金额:
    --
  • 项目类别:

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