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Related Concept Videos

Introduction to Mechanisms of Enzyme Catalysis01:13

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For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes...
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Enzymes02:34

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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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The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an enzyme-catalyzed reaction. Wilhelm Kuhne coined the term 'enzyme' in 1877 from the Greek words ‘en’ meaning ‘in’ or ‘within’ and ‘zyme’ meaning ‘yeast.’
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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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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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A role for conformational changes in enzyme catalysis.

Olivier Rivoire1

  • 1Gulliver, CNRS, ESPCI, Université PSL, Paris, France.

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|May 5, 2024
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Summary
This summary is machine-generated.

Enzyme catalysis can be enhanced by conformational changes, which overcome conflicting requirements for substrate binding and product release. A formal model shows how substrate "handles" and enzyme flexibility break this trade-off, improving catalytic efficiency.

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Area of Science:

  • Biochemistry
  • Chemical Kinetics
  • Enzyme Mechanisms

Background:

  • The role of enzyme conformational changes in catalysis is debated.
  • Formal models can elucidate conditions promoting catalysis via conformational changes.

Purpose of the Study:

  • To present a model explaining how conformational changes break a trade-off in catalytic cycles.
  • To identify the role of substrate "handles" in enzyme catalysis.

Main Methods:

  • Developed a formal model for irreversible one-step unimolecular reactions.
  • Analyzed catalysts with and without internal degrees of freedom.
  • Investigated two-state catalysts to overcome limitations.

Main Results:

  • Conformational changes can resolve conflicting requirements for transition state specificity and product release.
  • Substrate "handles" induce conformational transitions, essential for rapid catalytic cycles.
  • Chemical similarities between reaction states limit catalytic turnover, but multiple enzyme states overcome this.

Conclusions:

  • Enzyme conformational flexibility and substrate "handles" are crucial for efficient catalysis.
  • The model provides a formalism for understanding constraints in enzyme catalysis.
  • Findings align with challenges and observations in heterogeneous catalysis.