Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Preparation of Amines: Reductive Amination of Aldehydes and Ketones01:38

Preparation of Amines: Reductive Amination of Aldehydes and Ketones

4.1K
Carbonyl compounds and primary amines undergo reductive amination first to produce imines, followed by secondary amines in the same reaction mixture, using selective reducing agents like sodium cyanoborohydride or sodium triacetoxyborohydride. Reductive amination produces different degrees of substitution of amines depending on the starting amine substrate.
4.1K
Phase I Reactions: Reductive Reactions01:27

Phase I Reactions: Reductive Reactions

690
Phase I biotransformation reductive reactions are chemical processes that modify drugs by introducing or revealing polar functional groups via reduction. Enzymes called reductases catalyze these reactions, playing a pivotal role in drug metabolism by transforming lipophilic drugs into more polar, water-soluble metabolites for easy excretion. An essential type of reductive reaction is the carbonyl group reduction, where aldehydes and ketones are reduced to alcohols. An example is the...
690
Amides to Amines: LiAlH4 Reduction01:20

Amides to Amines: LiAlH4 Reduction

6.5K
Amide reduction with strong reducing agents like lithium aluminum hydride proceeds through a nucleophilic acyl substitution to form amines. Primary, secondary, and tertiary amides yield primary, secondary, and tertiary amines, respectively.
Amide reduction requires two equivalents of the reducing agent, acting as a source of hydride ions. As shown in the figure, the reaction is initiated with a nucleophilic attack by the hydride ion at the carbonyl carbon to form a tetrahedral intermediate.
6.5K
Nitriles to Amines: LiAlH4 Reduction00:55

Nitriles to Amines: LiAlH4 Reduction

4.9K
Nitriles are reduced to amines in the presence of strong reducing agents like lithium aluminum hydride through a typical nucleophilic acyl substitution. The reaction requires two equivalents of the reducing agent. The reducing agent acts as a source of hydride ions.
As shown below, the mechanism involves three steps. Firstly, the hydride ion acting as a nucleophile attacks the nitrile carbon to form an anion. In the second step, a second equivalent of the hydride ion attacks the anion to...
4.9K
Aldehydes and Ketones with Amines: Imine and Enamine Formation Overview01:16

Aldehydes and Ketones with Amines: Imine and Enamine Formation Overview

7.1K
Primary amines react with carbonyl compounds—aldehydes and ketones—to generate imines. Imines consist of a C=N double bond and are named Schiff bases after its discoverer—the German chemist Hugo Schiff. On the other hand, secondary amines react with carbonyl compounds to give enamines. In enamines, the presence of a C=C double bond adjacent to the nitrogen atom leads to the delocalization of the lone pair.
7.1K
Aldehydes and Ketones with Amines: Imine Formation Mechanism01:23

Aldehydes and Ketones with Amines: Imine Formation Mechanism

8.8K
Imine formation involves the addition of carbonyl compounds to a primary amine. It begins with the generation of carbinolamine through a series of steps involving an initial nucleophilic attack and then several proton transfer reactions. The second part includes the elimination of water, as a leaving group, to give the imine.
Imines are formed under mildly acidic conditions. A pH of 4.5 is ideal for the reaction.
If the pH is low or the solution is too acidic, the reaction slows down in the...
8.8K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Structure, characterisation and application of an unspecific peroxygenase from <i>Daldinia childiae</i>.

RSC chemical biology·2026
Same author

Nicotine biosynthesis is completed by cryptic activating glucosylation.

Nature communications·2026
Same author

Biocatalytic cascades enable manufacture of the macrocyclic peptide enlicitide.

Science (New York, N.Y.)·2026
Same author

Stereoselective Biotransformation: Transfer of Learning to Advance Drug Metabolism and Biocatalysis.

Angewandte Chemie (International ed. in English)·2026
Same author

Biocatalytic Production of a Key Chiral Intermediate of the HIV Capsid Inhibitor Lenacapavir.

Journal of the American Chemical Society·2026
Same author

Enhanced secretion of an Agrocybe aegerita peroxygenase variant in K. phaffii using the native signal peptide.

AMB Express·2026
Same journal

Function through shape: An overview of DNA G-quadruplexes in transcriptional regulation.

Current opinion in chemical biology·2026
Same journal

Advances in tools and technologies for multiplexed bioluminescence imaging.

Current opinion in chemical biology·2026
Same journal

High-resolution molecular mapping by expansion-coupled label-free and multimodal imaging.

Current opinion in chemical biology·2026
Same journal

Recent advances in glycoconjugate-based therapeutics.

Current opinion in chemical biology·2026
Same journal

Towards better red emitters for bioimaging: Innovations in rhodamine and cyanine chemistry.

Current opinion in chemical biology·2026
Same journal

Chemigenetic fluorescent biosensors in biological imaging - New trends and advances.

Current opinion in chemical biology·2026
See all related articles

Related Experiment Video

Updated: Mar 9, 2026

Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins
13:59

Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins

Published on: December 12, 2013

6.7K

Imine reductases (IREDs).

Juan Mangas-Sanchez1, Scott P France1, Sarah L Montgomery1

  • 1School of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester M1 7DN, UK.

Current Opinion in Chemical Biology
|December 31, 2016
PubMed
Summary
This summary is machine-generated.

Imine reductases (IREDs) are powerful biocatalysts for creating optically active amines. Recent advances in bioinformatics have expanded the toolkit of available IREDs for diverse synthetic applications.

More Related Videos

Imine Metathesis by Silica-Supported Catalysts Using the Methodology of Surface Organometallic Chemistry
09:37

Imine Metathesis by Silica-Supported Catalysts Using the Methodology of Surface Organometallic Chemistry

Published on: October 18, 2019

10.2K
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

12.8K

Related Experiment Videos

Last Updated: Mar 9, 2026

Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins
13:59

Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins

Published on: December 12, 2013

6.7K
Imine Metathesis by Silica-Supported Catalysts Using the Methodology of Surface Organometallic Chemistry
09:37

Imine Metathesis by Silica-Supported Catalysts Using the Methodology of Surface Organometallic Chemistry

Published on: October 18, 2019

10.2K
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

12.8K

Area of Science:

  • Biocatalysis
  • Organic Synthesis
  • Enzymology

Background:

  • Imine reductases (IREDs) are increasingly recognized as key enzymes for asymmetric amine synthesis.
  • Bioinformatics and database development have accelerated the discovery of novel IRED biocatalysts.
  • IREDs offer a sustainable and efficient alternative to traditional chemical catalysts.

Purpose of the Study:

  • To review recent advancements in the structural and mechanistic understanding of imine reductases.
  • To highlight the diverse synthetic applications of IREDs in modern organic chemistry.
  • To identify current challenges and future directions in IRED research and development.

Main Methods:

  • Literature review of recent studies on imine reductases.
  • Analysis of structural and mechanistic data from characterized IREDs.
  • Compilation of synthetic applications and case studies involving IREDs.

Main Results:

  • Detailed insights into the structural features and catalytic mechanisms of various IREDs.
  • Demonstration of IREDs' versatility in synthesizing a wide range of optically active amines.
  • Identification of key factors influencing IRED activity, selectivity, and stability.

Conclusions:

  • Imine reductases represent a rapidly evolving class of biocatalysts with significant potential in asymmetric synthesis.
  • Continued research into IRED structure-function relationships will unlock new catalytic capabilities.
  • Addressing challenges in enzyme engineering and process optimization will further enhance the industrial applicability of IREDs.