Related Experiment Video
Updated: May 12, 2026

08:10
Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System
Published on: August 8, 2016
EnzymeMiner 2.0: advancing automated enzyme discovery with expansive sequence mining and smart property analysis
Monika Rosinska1,2, Lucie Svobodova1,3, Simeon Borko1,2
1Loschmidt Laboratories, Department of Experimental Biology & RECETOX, Faculty of Science, Masaryk University, Brno, 625 00, Czech Republic.
Nucleic Acids Research
|May 11, 2026
Summary
EnzymeMiner 2.0 enhances enzyme discovery by expanding its protein database and adding predictive features for properties like melting temperature and pH. This tool accelerates finding novel enzymes with desired catalytic activities.
Area of Science:
- Biotechnology and Bioinformatics
- Enzyme Engineering
- Computational Biology
Background:
- Enzyme enhancement is crucial but costly and time-consuming.
- Identifying enzymes with specific catalytic activities and improved properties from sequence databases is an efficient strategy.
- The original EnzymeMiner web server facilitated enzyme discovery based on sequence and essential residues.
Purpose of the Study:
- Introduce EnzymeMiner 2.0, an upgraded web server for enzyme discovery.
- Expand the capabilities of the original EnzymeMiner tool.
- Provide enhanced features for identifying and prioritizing novel enzymes.
Main Methods:
- Expanded the searchable protein sequence database.
- Integrated state-of-the-art computational tools for predicting enzyme properties (melting temperature, optimal pH, aggregation propensity).
- Implemented smart automatic prioritization and filtering based on user-defined objectives.
Main Results:
- EnzymeMiner 2.0 offers a significantly larger searchable protein space.
- Provides comprehensive annotations including predicted melting temperature, optimal pH, catalytic efficiency, and aggregation propensity.
- Features intelligent prioritization and filtering for efficient enzyme candidate selection.
Conclusions:
- EnzymeMiner 2.0 represents a significant advancement in automated enzyme discovery.
- The enhanced features streamline the identification of novel enzymes with desired properties.
- The tool aims to be a leading solution for efficient enzyme engineering and discovery.
Related Concept Videos
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...
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...
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.
Enzyme Kinetics
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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Enzyme-linked Receptors
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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...
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...
