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Ribozymes

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.
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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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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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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.

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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.
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Restriction Enzymes

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Restriction enzymes are bacterial enzymes used to cut DNA in a sequence-specific manner. To cleave DNA, they bind to specific palindromic sequences called restriction sites. Such palindromic DNA sequences or inverted repeats are commonly found in regions of functional significance, such as the origin of replication, gene operator sites, and regions containing transcription termination signals.
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Decoupling Activity and Specificity in Coronazymes.

Jiahao Ji¹, Li Zuo^1,2, Bishal Pokhrel¹

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

Small (Weinheim an Der Bergstrasse, Germany)

|March 4, 2025

Summary

This summary is machine-generated.

This study introduces novel coronazymes, artificial enzymes combining gold nanoparticles and DNA aptamers. These engineered enzymes show enhanced activity and tunable specificity, decoupling key properties for superior catalyst design.

Keywords:

CISS activity and specificity chiral modulation modular design mosaicking

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Published on: June 30, 2019

Area of Science:

Nanotechnology and Materials Science
Biochemistry and Enzyme Engineering
Chirality and Photonics

Background:

Natural enzymes often face a trade-off between specificity and catalytic activity.
Developing artificial enzymes with decoupled activity and specificity is a key challenge in nanotechnology.
Gold nanoparticles (AuNPs) and DNA aptamers offer versatile platforms for creating novel nanozymes.

Purpose of the Study:

To engineer and characterize coronazymes (AuNP core with DNA aptamer corona) for glucose substrates.
To investigate the decoupling of catalytic activity and chiral specificity in these artificial enzymes.
To explore the influence of circularly polarized light (CPL) on coronazyme chiral specificity.

Main Methods:

Fabrication of AuNP-DNA aptamer coronazymes for glucose detection.
Single-molecule fluorescent magnetic tweezers coupled with highly inclined and laminated optical sheet (MT-HILO) microscopy.
Investigation of coronazyme activity with d-glucose and l-glucose.
Assessment of long-range modulation of specificity by circularly polarized light (CPL) and chiral induced spin selectivity (CISS).

Main Results:

Coronazymes exhibited approximately 30-fold higher catalytic activity compared to bare AuNP nanozymes.
Chiral specificity was modulated by CPL, following the chiral induced spin selectivity (CISS) principle.
Surprisingly, coronazymes catalyzed l-glucose more effectively than d-glucose, despite aptamer evolution for d-glucose.

Conclusions:

Demonstrated the first artificial enzyme with activity controlled by short-range forces and chiral specificity modulated by long-range CPL.
The decoupled design allows separate optimization of activity and specificity, surpassing natural enzyme limitations.
This approach is pivotal for creating advanced catalysts with superior performance characteristics.