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Related Concept Videos

Allosteric Regulation01:08

Allosteric Regulation

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Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
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Allosteric Proteins-ATCase01:19

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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
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Ligand Binding and Linkage00:49

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Cooperative Allosteric Transitions01:58

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Feedback Inhibition00:46

Feedback Inhibition

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Biochemical reactions are occurring constantly in cells, converting starting substances to different products, usually with the help of enzymes that speed the reactions. Without enzymes, it would take far too long for most reactions to occur to be useful to the cell!
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Enzymes02:34

Enzymes

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Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
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Related Experiment Video

Updated: Jun 4, 2025

Aptamer-Based Target Detection Facilitated by a 3-Stage G-Quadruplex Isothermal Exponential Amplification Reaction
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Examining Arginase-1 Trimerization Uncovers a Promising Allosteric Site for Inhibition.

Juhans Dechenne1, Magdalena Wierzbicka2, Reda Krimou1

  • 1Louvain Drug Research Institute (LDRI), Medicinal Chemistry Research Group (CMFA), Université Catholique de Louvain (UCLouvain), Brussels B-1200, Belgium.

Journal of Medicinal Chemistry
|January 3, 2025
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Summary

Researchers found that only trimeric Arginase-1 (ARG-1) is active. Targeting ARG-1

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A Semi-High-Throughput Adaptation of the NADH-Coupled ATPase Assay for Screening Small Molecule Inhibitors
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A Semi-High-Throughput Adaptation of the NADH-Coupled ATPase Assay for Screening Small Molecule Inhibitors
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Area of Science:

  • Biochemistry
  • Enzymology
  • Cancer Immunotherapy

Background:

  • Arginase-1 (ARG-1) is a key target in cancer immunotherapy.
  • Inhibitor development for ARG-1 is challenging due to its small, polar active site.
  • Targeting protein oligomerization offers an alternative inhibition strategy.

Purpose of the Study:

  • To investigate the role of ARG-1 oligomerization in its activity.
  • To identify allosteric sites regulating ARG-1 trimerization.
  • To validate a novel approach for ARG-1 inhibition by disrupting its oligomeric structure.

Main Methods:

  • Production of monomeric arginase-1 to confirm trimer dependency.
  • In silico-driven site-directed mutagenesis to identify key residues for trimerization.
  • Chemical modification using phenylglyoxal to disrupt oligomerization.

Main Results:

  • Only trimeric ARG-1 exhibits enzymatic activity.
  • An allosteric site involving five amino acids was identified as crucial for ARG-1 trimerization.
  • Phenylglyoxal covalently modified a key arginine residue, disrupting ARG-1 oligomerization.

Conclusions:

  • ARG-1 activity is dependent on its trimeric state.
  • Allosteric targeting of the ARG-1 trimerization site is a viable strategy for enzyme inhibition.
  • Disruption of ARG-1 homomeric structure validates a novel therapeutic approach for cancer immunotherapy.