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Related Concept Videos

Reaction Mechanisms03:06

Reaction Mechanisms

Chemical reactions often occur in a stepwise fashion, involving two or more distinct reactions taking place in a sequence. A balanced equation indicates the reacting species and the product species, but it reveals no details about how the reaction occurs at the molecular level. The reaction mechanism (or reaction path) provides details regarding the precise, step-by-step process by which a reaction occurs.
For instance, the decomposition of ozone appears to follow a mechanism with two steps:
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...
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.
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...
Woodward–Hoffmann Selection Rules and Microscopic Reversibility01:34

Woodward–Hoffmann Selection Rules and Microscopic Reversibility

Electrocyclic reactions, cycloadditions, and sigmatropic rearrangements are concerted pericyclic reactions that proceed via a cyclic transition state. These reactions are stereospecific and regioselective. The stereochemistry of the products depends on the symmetry characteristics of the interacting orbitals and the reaction conditions. Accordingly, pericyclic reactions are classified as either symmetry-allowed or symmetry-forbidden. Woodward and Hoffmann presented the selection criteria for...
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: Jun 30, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Do enzymes obey the Baldwin rules? A mechanistic imperative in enzymatic cyclization reactions.

J A Piccirilli1

  • 1Howard Hughes Medical Institute, Departments of Biochemistry, The University of Chicago, 5841 South Maryland Avenue, MC 1028, Chicago, IL 60637, USA. jpicciri@midway uchicago.edu

Chemistry & Biology
|March 13, 1999
PubMed
Summary
This summary is machine-generated.

Enzymes may follow the same chemical rules as reactions in solution. This study proposes using principles from organic chemistry to analyze enzyme-catalyzed cyclization reactions.

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Last Updated: Jun 30, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

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Published on: January 16, 2016

Enzymatic Cascade Reactions for the Synthesis of Chiral Amino Alcohols from L-lysine
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Published on: February 16, 2018

Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks (MOFs)
08:25

Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks (MOFs)

Published on: January 17, 2020

Area of Science:

  • Biochemistry
  • Organic Chemistry
  • Enzymology

Background:

  • Enzymes are believed to operate under fundamental energetic and stereoelectronic principles governing solution-phase reactions.
  • Understanding these principles is key to deciphering enzyme mechanisms.

Purpose of the Study:

  • To hypothesize how principles of organic ring-closure reactions can be applied to enzyme-catalyzed cyclization.
  • To provide a framework for analyzing enzymatic cyclization mechanisms.

Main Methods:

  • Review and application of established principles from organic reaction mechanisms.
  • Development of a theoretical framework for enzyme-catalyzed cyclizations.

Main Results:

  • The study proposes a hypothesis linking organic reaction principles to enzyme catalysis.
  • A potential framework for analyzing enzyme-catalyzed cyclization is outlined.

Conclusions:

  • Enzyme-catalyzed cyclization reactions may be understood through the lens of organic chemistry principles.
  • This approach offers a novel perspective for studying enzyme mechanisms and evolution.