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Related Concept Videos

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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Updated: Jun 24, 2025

Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System
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Environmental activity-based protein profiling for function-driven enzyme discovery from natural communities.

Sabrina Ninck1, Thomas Klaus2, Tatiana V Kochetkova3

  • 1Chemical Biology, Centre of Medical Biotechnology (ZMB), Faculty of Biology, University of Duisburg-Essen, Universitätsstr. 2, 45117, Essen, Germany. sabrina.ninck@uni-due.de.

Environmental Microbiome
|June 3, 2024
PubMed
Summary
This summary is machine-generated.

Environmental activity-based protein profiling (eABPP) identifies active microbial enzymes directly in their natural habitats. This novel multi-omics approach aids in discovering new biocatalysts and understanding microbial ecology without relying on sequence homology.

Keywords:
Activity-based protein profilingChemical proteomicsClick chemistryEnvironmental microbial communitiesHot springsMetagenomicsMetaproteomicsSerine hydrolasesTarget identification

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Determination of Microbial Extracellular Enzyme Activity in Waters, Soils, and Sediments using High Throughput Microplate Assays
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Area of Science:

  • Microbiology
  • Biochemistry
  • Ecology

Background:

  • Microbial communities drive essential biogeochemical cycles and possess vast, largely uncharacterized enzymatic potential.
  • Discovering novel enzymes from extreme environments is crucial for biotechnology, but accurately predicting function and in vivo activity remains challenging.
  • Current bioprospecting relies on metagenomics and bioinformatics, often limited by the need for sequence homology.

Purpose of the Study:

  • To introduce environmental activity-based protein profiling (eABPP) as a method to directly identify active enzymes in environmental samples.
  • To bridge the gap between environmental genomics, accurate function annotation, and in vivo enzyme activity.
  • To showcase eABPP's capability in discovering functional enzymes from extreme habitats.

Main Methods:

  • Developed and applied environmental activity-based protein profiling (eABPP), a multi-omics approach.
  • Integrated genome-resolved metagenomics with mass spectrometry-based activity-based protein profiling (ABPP).
  • Analyzed microbial communities from natural hot spring environments.

Main Results:

  • Successfully profiled active enzymes directly within environmental community samples in their native habitats.
  • Identified active enzymes based on their function, independent of sequence or structural homology.
  • Reported the discovery of active thermostable serine hydrolases from hot spring microbial communities.

Conclusions:

  • eABPP enables reporting of enzyme activities within ecosystems in their native state.
  • This method advances enzyme discovery for biocatalyst development by overcoming sequence homology limitations.
  • eABPP contributes to ecological research by dissecting microbial community interactions and their molecular mechanisms.