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Related Concept Videos

Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

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...
Enzyme Kinetics01:19

Enzyme Kinetics

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.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

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 a mild...
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Enzymes02:34

Enzymes

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.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...

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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
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Published on: January 16, 2016

Chemoenzymatic and microbial dynamic kinetic resolutions.

Azlina Harun Kamaruddin1, Mohamad Hekarl Uzir, Hassan Y Aboul-Enein

  • 1School of Chemical Engineering, Engineering Campus, Universiti Sains Malaysia, Pulau Pinang, Malaysia. chazlina@eng.usm.my

Chirality
|July 26, 2008
PubMed
Summary
This summary is machine-generated.

This review highlights a decade of advances in dynamic kinetic resolution, emphasizing biocatalysis for efficient synthesis. Future research should address scale-up challenges by considering early-stage factor extraction.

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Area of Science:

  • Organic Chemistry
  • Biocatalysis
  • Green Chemistry

Background:

  • Dynamic kinetic resolution (DKR) is crucial for synthesizing enantiopure compounds.
  • Traditional DKR methods often involve multiple steps and harsh conditions.
  • Biocatalysis offers a greener and more efficient alternative for DKR.

Purpose of the Study:

  • To review the advancements in DKR over the past decade, focusing on biocatalytic approaches.
  • To highlight the benefits of enzymatic and microbial methods in DKR.
  • To identify key considerations for future DKR developments, particularly for scale-up.

Main Methods:

  • Literature review of DKR studies from the last 10 years.
  • Focus on methods employing enzymatic or microbial catalysts for the resolution step.
  • Analysis of racemization techniques, including enzymatic and chemocatalytic options.

Main Results:

  • Biocatalytic DKR significantly reduces synthetic steps compared to conventional methods.
  • Enzymatic and microbial catalysts enable efficient and selective kinetic resolution.
  • Combined biocatalytic resolution and racemization streamline synthetic pathways.

Conclusions:

  • Biocatalysis is a powerful tool for advancing dynamic kinetic resolution.
  • Future DKR strategies must proactively address scale-up issues by considering early-stage factors to prevent inhibition.
  • Continued innovation in biocatalytic DKR promises more sustainable and efficient synthesis of chiral molecules.