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Related Concept Videos

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...
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...
Enzyme Kinetics01:19

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...
Other Glycolytic Pathways01:24

Other Glycolytic Pathways

The pentose phosphate pathway (PPP) operates in parallel with glycolysis, facilitating the metabolism of both pentoses and glucose. This pathway consists of two distinct phases: the oxidative and non-oxidative phases. While it does not directly generate ATP, the intermediates formed during the process can integrate into glycolysis, contributing to cellular energy metabolism when required.Oxidative Phase: NADPH ProductionThe oxidative phase of the pentose phosphate pathway is primarily...
Introduction to Enzymes01:22

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...
Introduction To Enzymes01:22

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...

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Related Experiment Video

Updated: May 14, 2026

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules
10:23

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules

Published on: April 25, 2025

Flexibility and reactivity in promiscuous enzymes.

Pietro Gatti-Lafranconi1, Florian Hollfelder

  • 1Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, UK.

Chembiochem : a European Journal of Chemical Biology
|January 31, 2013
PubMed
Summary

Enzymes achieve both promiscuity and efficiency through a balance of active site chemical reactivity and protein structural flexibility. This review explores how these factors influence enzyme catalysis.

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Last Updated: May 14, 2026

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Published on: November 23, 2016

Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Enzymes exhibit both promiscuity and efficiency, a seemingly paradoxical combination.
  • The dynamic nature of proteins and the reactivity of active sites are key factors in enzyme function.

Purpose of the Study:

  • To analyze the interplay between protein structural flexibility and active site chemical reactivity.
  • To elucidate the roles of these factors in the catalytic mechanisms of selected enzymes.

Main Methods:

  • Literature review of enzymatic catalysis.
  • Analysis of structural dynamics and chemical reactivity in enzyme mechanisms.

Main Results:

  • Structural flexibility allows enzymes to adapt to various substrates, contributing to promiscuity.
  • Active site chemical reactivity is crucial for catalytic efficiency, enabling rapid transformations.
  • The dynamic character of proteins can fine-tune active site properties for optimal catalysis.

Conclusions:

  • The combination of protein dynamics and active site reactivity provides a unified explanation for enzyme promiscuity and efficiency.
  • Understanding this interplay is essential for enzyme engineering and drug design.