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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

Introduction to Mechanisms of Enzyme Catalysis

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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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Restriction Enzymes01:11

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.
The host bacteria protect their own genomic DNA from these enzymes by methylating these sites. Some...
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Enzyme Kinetics01:19

Enzyme Kinetics

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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.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
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DNA Topoisomerases02:02

DNA Topoisomerases

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Topoisomerases are enzymes that relax overwound DNA molecules during various cell processes, including DNA replication and transcription. These enzymes regulate positive and negative DNA supercoiling without changing the nucleotide sequence. DNA overwinding in a clockwise direction results in positively supercoiled DNA, whereas underwinding in a counterclockwise direction produces negatively supercoiled DNA.
Types and Mechanism of action
Topoisomerases are divided into two main types. ...
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Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

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For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
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Author Spotlight: Advancements in DNA Nanosensors – Addressing Sensitivity and Selectivity Challenges in Molecular Detection
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DNA-crowded enzyme complexes with enhanced activities and stabilities.

John Collins1, Ting Zhang, Sung Won Oh

  • 1Department of Chemistry, Rutgers University - Camden, Camden, NJ 08102, USA. jinglin.fu@rutgers.edu.

Chemical Communications (Cambridge, England)
|November 23, 2017
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Summary

Researchers developed DNA-crowded enzyme complexes using DNA duplexes for enhanced stability and activity. These novel enzyme complexes show potential for biomaterials and biotechnology applications.

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Area of Science:

  • Biochemistry
  • Biotechnology
  • Materials Science

Background:

  • Enzyme engineering aims to improve enzyme performance for industrial applications.
  • Current methods for enzyme stabilization and activity enhancement are often complex or limited.
  • DNA nanotechnology offers novel strategies for biomolecular complex assembly.

Purpose of the Study:

  • To develop a simple and robust method for creating DNA-crowded enzyme complexes.
  • To investigate the impact of DNA crowding on enzyme activity and stability.
  • To explore the potential applications of these engineered enzyme complexes.

Main Methods:

  • Direct assembly of long DNA duplexes onto enzyme surfaces.
  • Characterization of DNA-crowded enzyme complex structure and properties.
  • Assays to measure substrate turnover numbers and enzyme stability under various conditions.

Main Results:

  • Successfully prepared DNA-crowded enzyme complexes with a straightforward protocol.
  • Observed significantly boosted substrate turnover numbers in the DNA-crowded complexes.
  • Demonstrated increased enzyme stability against diverse storage conditions.

Conclusions:

  • The developed method provides a robust approach to engineer enzyme complexes with enhanced catalytic efficiency and stability.
  • DNA-crowded enzyme complexes represent a promising platform for advanced biomaterials and biotechnological applications.
  • The scalability of this method suggests broad applicability in enzyme-based industrial processes.