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Related Concept Videos

Cofactors and Coenzymes01:24

Cofactors and Coenzymes

Enzymes are proteins made of amino acids. The functional group of each constituent amino acid catalyzes a wide variety of chemical reactions via ionic interactions or acid-base reactions. However, amino acids cannot catalyze oxidation-reduction and group transfer reactions and need to be aided by non-protein components called cofactors. Cofactors are also referred to as the chemical teeth of an enzyme.
Cofactors can be metallic ions or organic molecules called coenzymes. These types of helper...
Cofactors and Coenzymes01:27

Cofactors and Coenzymes

Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.
Cofactors and Coenzymes01:27

Cofactors and Coenzymes

Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

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 a mild...
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

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 a mild...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

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Related Experiment Video

Updated: Jun 10, 2026

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
09:27

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability

Published on: April 22, 2016

The CoFactor database: organic cofactors in enzyme catalysis.

Julia D Fischer1, Gemma L Holliday, Janet M Thornton

  • 1EMBL-EBI, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, UK. julia.fischer@ebi.ac.uk

Bioinformatics (Oxford, England)
|August 4, 2010
PubMed
Summary

The CoFactor database offers curated information on organic enzyme cofactors, crucial for understanding enzyme catalysis. This resource aids researchers by detailing cofactor variations and associated enzyme structures.

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EPR Monitored Redox Titration of the Cofactors of Saccharomyces cerevisiae Nar1
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Published on: April 22, 2016

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Bioinformatics

Background:

  • Organic enzyme cofactors are essential for numerous enzymatic reactions.
  • Analyzing cofactors is key to understanding enzyme catalysis mechanisms.
  • A comprehensive resource for cofactor data was lacking.

Purpose of the Study:

  • To develop a centralized database for organic enzyme cofactors.
  • To provide researchers with easy access to curated cofactor information.
  • To facilitate a deeper understanding of enzyme-biocatalysis.

Main Methods:

  • Compilation of hand-curated data from scientific literature.
  • Integration of automatically collected information on cofactors.
  • Development of a user-friendly web interface for data access.

Main Results:

  • The CoFactor database is now publicly available.
  • It contains detailed information on enzyme-bound organic cofactors.
  • Includes data on cofactor conformation, solvent accessibility, and hosting enzyme structures/mechanisms.

Conclusions:

  • The CoFactor database serves as a valuable resource for researchers in enzymology and biocatalysis.
  • It enhances the study of enzyme mechanisms by providing integrated cofactor data.
  • The database supports advancements in understanding and utilizing enzyme catalysis.