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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.
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Ribozymes02:47

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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.
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Catalytically Perfect Enzymes01:07

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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.
 
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Protein Complexes with Interchangeable Parts01:57

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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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Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System
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Mimicomes: Mimicking Multienzyme System by Artificial Design.

Haolin Cao1, Jing Jiang1, Lei Chen1,2

  • 1CAS Engineering Laboratory for Nanozyme, Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.

Advanced Healthcare Materials
|October 9, 2024
PubMed
Summary
This summary is machine-generated.

Artificial cascade systems, or mimicomes, are engineered to replicate natural enzyme functions. This review explores their evolution from enzyme-based to nanozyme and hybrid systems, highlighting their potential in medicine.

Keywords:
artificial designcascade reactionsmimicomesmultienzyme complexnanozymes

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Area of Science:

  • Biochemistry
  • Nanotechnology
  • Biomedical Engineering

Background:

  • Enzymes are crucial cellular catalysts organized in cascade systems for biochemical processes.
  • Dysfunction of natural cascade systems is linked to various diseases.
  • Nanotechnology enables the creation of artificial systems mimicking natural enzyme cascades.

Purpose of the Study:

  • Introduce and define the concept of mimicomes: artificial cascade catalytic systems.
  • Review the evolution and development of different types of mimicomes.
  • Summarize challenges and future prospects of mimicomes.

Main Methods:

  • Literature review and synthesis of research on artificial cascade systems.
  • Categorization of mimicomes based on their components (enzyme-based, nanozyme-based, hybrid).
  • Analysis of the functional mimicry and efficiency of described systems.

Main Results:

  • Mimicomes effectively replicate natural cascade systems' functions.
  • Evolution includes enzyme-based (immobilized, vesicle), nanozyme-based, and hybrid systems.
  • These systems offer enhanced catalytic efficiency and potential for in vitro/in vivo applications.

Conclusions:

  • Mimicomes represent a significant advancement in artificial enzyme catalysis.
  • Further research is needed to address challenges in designing multifunctional mimicomes.
  • Mimicomes hold promise for diverse applications, particularly in disease treatment and biochemical research.