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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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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 turnover number of an enzyme is the maximum number of substrate molecules it can transform per unit time. Turnover numbers for most enzymes range from 1 to 1000 molecules per second. Catalase has the known highest turnover number, capable of converting up to 2.8×106 molecules of hydrogen peroxide into water and oxygen per second. Lysozyme has the lowest known turnover number of half a molecule per second.
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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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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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DNA Catalysis: Design, Function, and Optimization.

Rebecca L Stratton1, Bishal Pokhrel1, Bryce Smith1

  • 1Department of Chemistry and Biochemistry, Kent State University, Kent, OH 44242, USA.

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|November 9, 2024
PubMed
Summary
This summary is machine-generated.

DNA catalysts, or DNAzymes, offer tunable and specific catalytic functions. This review covers traditional DNAzymes and novel DNAzyme hybrids, highlighting their performance and optimization for advanced applications.

Keywords:
DNA catalysisDNA-nanoparticle hybridDNAzymedesignfunctionoptimization

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Area of Science:

  • Biochemistry
  • Catalysis
  • Molecular Biology

Background:

  • Catalytic DNA (DNAzymes) are increasingly recognized for their efficiency, specificity, and tunability.
  • DNA's structural complexity allows for diverse functions beyond genetic storage, including catalysis.
  • Advancements in spectroscopy aid in understanding DNA catalyst mechanisms.

Purpose of the Study:

  • To review the performance and optimization strategies for traditional DNAzymes.
  • To analyze the unique properties and potential of DNAzyme hybrid catalysts.
  • To provide an in-depth overview of recent developments in DNA catalysis.

Main Methods:

  • Literature review of recent studies on DNAzymes and DNAzyme hybrids.
  • Analysis of spectroscopic techniques for mechanistic insights.
  • Synthesis of information on catalyst performance and optimization.

Main Results:

  • DNAzymes exhibit a wide range of catalytic activities, including electrocatalysis and enantioselectivity.
  • DNAzyme hybrids present novel and promising catalytic properties.
  • Rational structural optimization enhances DNA catalyst performance.

Conclusions:

  • Catalytic DNA represents a powerful platform for developing efficient and specific catalysts.
  • Further research into DNAzyme hybrids will unlock new catalytic applications.
  • Understanding DNA catalyst mechanisms is key to future optimization and design.