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Related Concept Videos

Allosteric Regulation01:08

Allosteric Regulation

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...
Allosteric Regulation01:08

Allosteric Regulation

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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

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 pathway,...

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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

Allosteric modulation of monomeric proteins*.

Paolo Ascenzi1, Alessio Bocedi, Alessandro Bolli

  • 1Dipartimento di Biologia and Laboratorio Interdipartimentale di Microscopia Elettronica, Università "Roma Tre," Viale Guglielmo Marconi 446, I-00146 Roma, Italy; Istituto Nazionale per le Malattie Infettive I.R.C.C.S. "Lazzaro Spallanzani," Via Portuense 292, I-00149 Roma, Italy. ascenzi@uniroma3.it.

Biochemistry and Molecular Biology Education : a Bimonthly Publication of the International Union of Biochemistry and Molecular Biology
|June 4, 2011
PubMed
Summary

Monomeric proteins like myoglobin may exhibit allosteric properties, challenging the traditional view. This study examines allosteric effectors in sperm whale myoglobin, human serum albumin, and human alpha-thrombin.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Science

Background:

  • Multimeric proteins, such as hemoglobin, are typically viewed as archetypal allosteric enzymes.
  • Monomeric proteins, like myoglobin, have traditionally been considered nonallosteric.
  • The influence of heterotropic allosteric effectors on monomeric protein function raises questions about this classification.

Purpose of the Study:

  • To investigate the allosteric properties of specific monomeric proteins.
  • To challenge the conventional understanding of allosteric regulation in proteins.
  • To summarize existing knowledge on the allosteric behavior of selected monomeric models.

Main Methods:

  • Literature review and synthesis of existing research.
  • Analysis of functional modulation by heterotropic allosteric effectors.
  • Focus on well-characterized monomeric protein models.

Main Results:

  • Evidence suggests that monomeric proteins can be modulated by allosteric effectors.
  • Sperm whale myoglobin, human serum albumin, and human alpha-thrombin exhibit allosteric characteristics.
  • The distinction between multimeric and monomeric proteins regarding allostery may be less rigid than previously thought.

Conclusions:

  • Monomeric proteins can display allosteric behavior, contrary to prior assumptions.
  • The study highlights the need to reconsider the definition and scope of allosteric regulation.
  • Selected monomeric proteins serve as valuable models for studying allosteric mechanisms.