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Related Concept Videos

Catalytically Perfect Enzymes01:07

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 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...
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...
Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
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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Updated: Jun 14, 2026

DNA-Tethered RNA Polymerase for Programmable In vitro Transcription and Molecular Computation
09:26

DNA-Tethered RNA Polymerase for Programmable In vitro Transcription and Molecular Computation

Published on: December 29, 2021

Computational enzymology.

Richard Lonsdale1, Kara E Ranaghan, Adrian J Mulholland

  • 1Centre for Computational Chemistry, School of Chemistry, University of Bristol, Bristol, UK BS8 1TS.

Chemical Communications (Cambridge, England)
|March 24, 2010
PubMed
Summary
This summary is machine-generated.

Molecular simulations offer atomic-level insights into enzyme mechanisms. This computational enzymology approach is advancing catalysis theories and aiding experimental studies, catalyst design, and drug development.

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Area of Science:

  • * Encompasses computational enzymology, utilizing molecular simulations and modeling.
  • * Focuses on understanding the fundamental mechanisms of biological catalysts at an atomic level.

Background:

  • * Molecular simulations and modeling are transforming the field of enzymology.
  • * Provides unprecedented atomic-level insights into enzyme catalysis.

Purpose of the Study:

  • * To explore how computational approaches are advancing enzymology.
  • * To highlight the role of molecular simulations in testing and refining catalytic theories.
  • * To identify novel catalytic mechanisms through computational analysis.

Main Methods:

  • * Application of molecular simulations and computational modeling techniques.
  • * Analysis of atomic-level interactions within enzyme active sites.
  • * Integration of computational findings with experimental enzymology studies.

Main Results:

  • * Detailed, atomic-level understanding of enzyme catalytic mechanisms.
  • * Validation and challenging of established enzymatic theories.
  • * Discovery of new catalytic pathways and mechanisms.
  • * Significant contributions to the interpretation of experimental data.

Conclusions:

  • * Computational enzymology is a rapidly advancing field with profound implications.
  • * Molecular modeling directly enhances experimental enzyme studies.
  • * Practical applications include catalyst design and drug development.