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Related Concept Videos

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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Related Experiment Video

Updated: Nov 21, 2025

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
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Self-Assembled Multimeric-Enzyme Nanoreactor for Robust and Efficient Biocatalysis.

Liang Yin1, Xiang Guo1, Lu Liu1

  • 1State Key Laboratory of Microbial Metabolism, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China.

ACS Biomaterials Science & Engineering
|January 13, 2021
PubMed
Summary
This summary is machine-generated.

Researchers developed stable multimeric enzyme nanoclusters (MENCs) using SpyTag/SpyCatcher technology for improved enzyme cascade performance. These nanoclusters enhance catalytic rates, stability, and reusability for applications in synthetic biology.

Keywords:
P450 monooxygenaseSpyCatcher/SpyTagglucose dehydrogenaseindigomultimeric enzymeself-assembly

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Area of Science:

  • Biocatalysis
  • Synthetic Biology
  • Nanotechnology

Background:

  • Enzyme cascades are crucial for biocatalysis, but their efficiency is limited by enzyme stability and spatial arrangement.
  • Developing stable, reusable multienzyme catalysts remains a significant challenge in enzyme engineering.

Purpose of the Study:

  • To create ultrastable multimeric enzyme nanoclusters (MENCs) for enhanced enzyme cascade performance.
  • To demonstrate a novel strategy for constructing self-assembled, covalently coupled supramolecular multienzyme nanodevices.

Main Methods:

  • Utilized the SpyTag/SpyCatcher system for orthogonal protein ligation.
  • Fused SpyCatcher to a dimeric cytochrome P450 monooxygenase mutant (P450BM3m) and SpyTag to a tetrameric glucose dehydrogenase (GDH).
  • Investigated the self-assembly, morphology, and catalytic activity of the resulting MENCs.

Main Results:

  • Successfully formed stable MENCs with a two-dimensional layerlike nanoscale architecture.
  • Achieved efficient NADPH regeneration and indole conversion to indigo.
  • Demonstrated a >3-fold increase in the initial rate of indigo synthesis.
  • Showcased significant improvements in MENC stability and reusability compared to free enzyme mixtures.

Conclusions:

  • The SpyTag/SpyCatcher system provides a versatile and efficient strategy for constructing stable, multifunctional biocatalysts.
  • MENCs offer enhanced performance and stability, showing promise for applications in metabolic engineering and synthetic biology.