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Related Concept Videos

Phase II Reactions: Methylation Reactions01:17

Phase II Reactions: Methylation Reactions

Methylation is a phase II biotransformation process involving the attachment of a methyl group to a substrate. Enzymes known as methyltransferases orchestrate this reaction.
The mechanism of methylation unfolds in two stages. The first stage sees a methyltransferase enzyme facilitating the transfer of a methyl group from S-adenosylmethionine (SAM) to the substrate, forming S-adenosylhomocysteine (SAH). The second stage involves further metabolism of SAH into homocysteine, which can be recycled...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

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Related Experiment Video

Updated: May 10, 2026

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
12:07

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues

Published on: November 22, 2014

Profiling protein methylation with cofactor analog containing terminal alkyne functionality.

Gil Blum1, Ian R Bothwell, Kabirul Islam

  • 1Molecular Pharmacology and Chemistry Program, Memorial Sloan-Kettering Cancer Center, New York, New York, USA.

Current Protocols in Chemical Biology
|June 22, 2013
PubMed
Summary
This summary is machine-generated.

Researchers developed a method using a modified S-adenosyl-L-methionine (SAM) cofactor, Se-adenosyl-L-selenomethionine (ProSeAM), to identify protein methyltransferase (PMT) substrates. This technique enables the profiling of endogenous PMT targets within cells.

Keywords:
ProSeAMSe‐adenosyl‐L‐selenomethionineazido‐azo biotin probeclick chemistry

More Related Videos

Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry (CCMS)
17:12

Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry (CCMS)

Published on: December 20, 2010

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells
08:11

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells

Published on: August 7, 2021

Related Experiment Videos

Last Updated: May 10, 2026

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
12:07

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues

Published on: November 22, 2014

Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry (CCMS)
17:12

Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry (CCMS)

Published on: December 20, 2010

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells
08:11

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells

Published on: August 7, 2021

Area of Science:

  • Biochemistry
  • Chemical Biology
  • Proteomics

Background:

  • Enzymatic transmethylation, crucial in biology and disease, involves S-adenosyl-L-methionine (SAM).
  • Identifying protein methyltransferase (PMT) substrates is essential for understanding cellular processes and disease mechanisms.

Purpose of the Study:

  • To develop a chemical biology approach for profiling endogenous PMT substrates in cellular contexts.
  • To utilize an alkyne-containing SAM mimic and a biotin probe for target identification.

Main Methods:

  • Preparation of cell lysates with active endogenous PMTs.
  • Labeling of PMT targets using Se-adenosyl-L-selenomethionine (ProSeAM), an alkyne-containing SAM analog.
  • Enrichment of labeled proteins via a cleavable azido-azo-biotin probe and reductive elution for proteomic analysis.

Main Results:

  • Successful profiling of endogenous PMT substrates using the ProSeAM chemical probe.
  • Demonstration of a robust protocol for target identification and proteomic analysis.

Conclusions:

  • The developed method enables the identification of protein methyltransferase substrates in cells.
  • The protocol is adaptable for other terminal-alkyne-containing SAM analog cofactors.