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Related Concept Videos

Induced-fit Model01:13

Induced-fit Model

Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical characteristics of...
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.
Enzymes02:34

Enzymes

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...
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...
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...
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...

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Related Experiment Video

Updated: May 12, 2026

Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System
08:10

Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System

Published on: August 8, 2016

Modular enzymes.

C Khosla1, P B Harbury

  • 1Department of Chemistry, Stanford University, California 94305, USA. ck.chemeng.stanford.edu

Nature
|February 24, 2001
PubMed
Summary
This summary is machine-generated.

Modular biocatalysts, including separable enzymes and multienzyme systems, are crucial in biology. Their recognition in biocatalysis offers new opportunities for synthetic and process chemistry.

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Area of Science:

  • Biocatalysis
  • Molecular Biology
  • Synthetic Chemistry

Background:

  • Modular macromolecular devices are common in biological systems.
  • The role of these modular structures in biocatalysis is often overlooked.
  • Understanding modularity is key to advancing enzyme applications.

Purpose of the Study:

  • To identify and categorize modular biocatalysts.
  • To highlight the significance of modular biocatalysts in biocatalysis.
  • To explore the potential impact of modular biocatalysts in synthetic and process chemistry.

Main Methods:

  • Classification of modular biocatalysts into three main groups.
  • Analysis of enzyme structure and function related to modularity.
  • Review of existing literature on modular biocatalysts.

Main Results:

  • Identified three classes of modular biocatalysts: separable catalysis/specificity enzymes, multisubstrate enzymes with modular binding sites, and multienzyme systems for metabolic pathways.
  • Demonstrated the prevalence and importance of modularity in biocatalysis.
  • Highlighted the potential for programmable metabolic pathways using multienzyme systems.

Conclusions:

  • Modular biocatalysts are a significant, underappreciated class of biological catalysts.
  • The identified classes provide a framework for understanding modular biocatalysis.
  • The postgenomic era offers new avenues for discovering and utilizing modular biocatalysts in chemistry.