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Related Concept Videos

Phase II Reactions: Acetylation Reactions01:24

Phase II Reactions: Acetylation Reactions

Acetylation, a phase II biotransformation reaction, introduces an acetyl group to drugs or their metabolites. Acetyltransferase enzymes facilitate this reaction, which resembles α-amino acid conjugation due to the addition of a functional group to the drug molecule.
The substrates for acetylation are typically drugs or their metabolites with an amino, sulfonamide, or hydrazine functional group. Acetylation can occur at several points in the drug molecule, including primary, secondary, and...
Amines to Amides: Acylation of Amines01:19

Amines to Amides: Acylation of Amines

Various carboxylic acid derivatives (such as acid chlorides, esters, and anhydrides) can be used for the acylation of amines to yield amides. The reaction requires two equivalents of amines. The first amine molecule functions as a nucleophile and attacks the carbonyl carbon to produce a tetrahedral intermediate. This is followed by the loss of the leaving group and restoration of the C=O bond.
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Acetoacetic ester synthesis is a method to obtain ketones from alkyl halides and β-keto esters. The reaction occurs in the presence of an alkoxide base that abstracts the acidic proton of the β-keto esters. The step results in an enolate ion which is doubly stabilized. The enolate then reacts with an alkyl halide via the SN2 process to produce an alkylated ester intermediate with a new C–C bond. The hydrolysis of the intermediate, followed by acidification, results in an alkylated β-keto acid.
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Preparation of Alkynes: Alkylation Reaction02:27

Preparation of Alkynes: Alkylation Reaction

Introduction
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A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
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Chemical acetylation and deacetylation.

Kristofer S Fritz1

  • 1Department of Pharmaceutical Sciences, Skaggs School of Pharmacy and Division of Cardiology, School of Medicine, University of Colorado Denver Anschutz Medical Center, Aurora, CO, USA.

Methods in Molecular Biology (Clifton, N.J.)
|September 10, 2013
PubMed
Summary

This study introduces a new in vitro method to study protein deacetylation. The technique uses chemical acetylation and mass spectrometry to analyze how lysine acetylation is reversed, aiding disease research.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Lysine acetylation is a crucial posttranslational modification impacting protein function.
  • Dysregulation of protein acetylation is implicated in various disease pathologies.
  • Understanding acetylation regulation is vital for disease mechanism elucidation.

Purpose of the Study:

  • To develop and validate an in vitro strategy for examining site-specific protein deacetylation.
  • To investigate the reversal of chemically induced lysine acetylation.
  • To provide a method for studying deacetylase activity, particularly SIRT3.

Main Methods:

  • Chemical acetylation of protein lysine residues using acetic anhydride.
  • Characterization of acetylation impact via native gel electrophoresis and Western blotting.
  • Assessment of deacetylation using SIRT3 deacetylase activity assays and stable isotope dilution mass spectrometry.

Main Results:

  • Successfully established an in vitro method for protein deacetylation studies.
  • Demonstrated the characterization of chemically induced acetyl-lysine modifications.
  • Validated the use of SIRT3 assays and mass spectrometry for analyzing deacetylation.

Conclusions:

  • The developed in vitro strategy enables detailed examination of protein deacetylation.
  • This method facilitates the study of enzymes like SIRT3 in reversing lysine acetylation.
  • Provides a valuable tool for understanding acetylation's role in health and disease.