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Related Concept Videos

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.
Synthetic Biology02:55

Synthetic Biology

Synthetic biology is an interdisciplinary science that involves using principles from disciplines such as engineering, molecular biology, cell biology, and systems biology. It involves remodeling existing organisms from nature or constructing completely new synthetic organisms for applications such as protein or enzyme production, bioremediation, value-added macromolecule production, and the addition of desirable traits to crops, to name a few.
Golden rice
Golden rice is a genetically modified...
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Ribozymes02:47

Ribozymes

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 be...
Introduction to Enzymes01:22

Introduction to Enzymes

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 bind the substrates and convert them into products. Many enzymes also...
Reduction of Alkenes: Asymmetric Catalytic Hydrogenation02:17

Reduction of Alkenes: Asymmetric Catalytic Hydrogenation

Catalytic hydrogenation of alkenes is a transition-metal catalyzed reduction of the double bond using molecular hydrogen to give alkanes. The mode of hydrogen addition follows syn stereochemistry.
The metal catalyst used can be either heterogeneous or homogeneous. When hydrogenation of an alkene generates a chiral center, a pair of enantiomeric products is expected to form. However, an enantiomeric excess of one of the products can be facilitated using an enantioselective reaction or an...

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Updated: Jun 6, 2026

Utilizing Thermal Shift Assay to Probe Substrate Binding to Selenoprotein O
03:09

Utilizing Thermal Shift Assay to Probe Substrate Binding to Selenoprotein O

Published on: August 9, 2024

Artificial selenoenzymes: designed and redesigned.

Xin Huang1, Xiaoman Liu, Quan Luo

  • 1State Key Laboratory for Supramolecular Structure and Materials, College of Chemistry, Jilin University, Changchun 130012, P. R. China.

Chemical Society Reviews
|December 3, 2010
PubMed
Summary
This summary is machine-generated.

Researchers are developing artificial enzymes that mimic nature's efficiency. This review details strategies for creating artificial selenoenzymes, focusing on glutathione peroxidase (GPx) active sites for antioxidant activity.

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Area of Science:

  • Biomimetic chemistry
  • Catalysis
  • Enzyme engineering

Background:

  • Enzymes are nature's catalysts, exhibiting high efficiency and specificity under mild conditions.
  • Significant research focuses on creating artificial enzyme-like catalysts using natural and synthetic host molecules.
  • A key challenge is achieving catalytic efficiencies and specificities comparable to natural enzymes.

Purpose of the Study:

  • To review methods and strategies for designing and redesigning artificial selenoenzymes.
  • To highlight the construction of active sites for antioxidative glutathione peroxidase (GPx).
  • To emphasize the principle of synergy between recognition and catalysis in artificial enzyme design.

Main Methods:

  • Rational design and manipulation of natural and synthetic host molecules.
  • Construction of active sites mimicking natural enzyme functions.
  • Focus on selenoenzyme engineering for antioxidant applications.

Main Results:

  • Demonstration of artificial systems achieving high efficiency and specificity rivaling natural enzymes.
  • Successful redesign of artificial selenoenzymes on various hosts.
  • Effective construction of GPx active sites through synergistic recognition and catalysis.

Conclusions:

  • Artificial selenoenzymes can be designed to rival natural enzymes in catalytic performance.
  • The synergy between recognition and catalysis is a key principle for designing effective artificial enzymes.
  • This review provides a roadmap for the development of advanced artificial enzymes for various applications.