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Related Concept Videos

Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

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Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
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Enzyme Kinetics01:19

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Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
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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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Introduction to Enzymes01:22

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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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Allosteric Regulation01:08

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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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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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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
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Loop dynamics and the evolution of enzyme activity.

Marina Corbella1, Gaspar P Pinto1,2, Shina C L Kamerlin3,4

  • 1Department of Chemistry, Uppsala University, Uppsala, Sweden.

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This summary is machine-generated.

Enzyme evolution is driven by conformational plasticity, particularly flexible loops. Manipulating these loops offers a powerful strategy for engineering enzyme activity and selectivity without altering active sites.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzyme Engineering

Background:

  • Enzyme evolution relies on conformational plasticity to expand functional diversity from limited sequences.
  • Conformational dynamics are increasingly recognized as crucial in natural and laboratory enzyme evolution.
  • Flexible protein loops play a key role in regulating enzyme activity and function.

Purpose of the Study:

  • To review the significance of flexible loops in enzyme activity regulation.
  • To showcase examples of loop dynamics in enzyme evolution and engineering.
  • To discuss the implications of manipulating loop dynamics for enzyme engineering.

Main Methods:

  • Review of existing literature on enzyme evolution and conformational dynamics.
  • Analysis of specific enzyme systems (e.g., triosephosphate isomerase, protein tyrosine phosphatases, β-lactamases).
  • Discussion of case studies involving the manipulation of protein loops for engineering purposes.

Main Results:

  • Flexible loops are critical for regulating enzyme activity, selectivity, and turnover.
  • Harnessing conformational (loop) dynamics has successfully manipulated protein function in various systems.
  • Loop manipulation can improve catalytic efficiency or alter enzyme selectivity.

Conclusions:

  • Manipulating the conformational dynamics of key protein loops is a powerful engineering strategy.
  • Tailoring enzyme activity can be achieved by mimicking nature through loop dynamics.
  • This approach offers an alternative to targeting active-site residues for enzyme modification.