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Related Concept Videos

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.
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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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

Introduction to Enzymes

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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.’
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that...
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Ribozymes02:47

Ribozymes

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The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can...
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Enzyme Inhibition01:30

Enzyme Inhibition

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Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
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Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

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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.
 
Most enzymes...
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Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
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Inorganic Enzyme Mimics.

Yihong Zhang1,2, Faheem Muhammad1,2, Hui Wei1,2

  • 1Department of Biomedical Engineering, College of Engineering and Applied Sciences, Nanjing National Laboratory of Microstructures, Jiangsu Key Laboratory of Artificial Functional Materials, Nanjing University, Nanjing, Jiangsu, 210023, P. R. China.

Chembiochem : a European Journal of Chemical Biology
|March 4, 2021
PubMed
Summary
This summary is machine-generated.

Enzyme mimics offer stable, cost-effective alternatives to natural enzymes. Inorganic materials, including complexes and nanomaterials, show promise for energy, environmental, and health applications.

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Area of Science:

  • Biochemistry
  • Materials Science
  • Nanotechnology

Background:

  • Enzyme mimics, or artificial enzymes, provide alternatives to natural enzymes.
  • They offer advantages like enhanced stability, reduced cost, and tunable activity.
  • Research has explored various materials for enzyme mimicry.

Discussion:

  • Inorganic materials, such as complexes and nanomaterials, are gaining attention for enzyme mimicry.
  • These inorganic enzyme mimics have demonstrated significant potential over the past decade.
  • Their development is driven by the need for advanced solutions in critical sectors.

Key Insights:

  • Inorganic enzyme mimics exhibit superior stability and cost-effectiveness compared to natural enzymes.
  • Tailorable activity allows for specific applications in diverse fields.
  • Nanomaterials represent a promising class of inorganic enzyme mimics.

Outlook:

  • Inorganic enzyme mimics are poised to address challenges in energy and environmental remediation.
  • Their application in healthcare, including diagnostics and therapeutics, is a key area for future research.
  • Continued innovation in inorganic nanomaterials will likely expand their enzymatic capabilities.