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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...
Pharmacogenetics of Phase II Enzymes: N-acetyltransferase, Thiopurine S-methyltransferase, UDP-glucuronosyltransferase01:27

Pharmacogenetics of Phase II Enzymes: N-acetyltransferase, Thiopurine S-methyltransferase, UDP-glucuronosyltransferase

Phase II biotransformation reactions are essential for detoxifying and eliminating xenobiotics, including many pharmaceutical compounds. These reactions typically involve conjugation, the covalent attachment of polar endogenous groups such as glucuronic acid, sulfate, methyl, or acetyl moieties to functional groups introduced during Phase I metabolism. The resulting conjugates are more water-soluble, enabling efficient renal or biliary excretion.The major classes of Phase II enzymes include...
Inborn Errors of Metabolism01:20

Inborn Errors of Metabolism

Phenylketonuria (PKU) is a protein metabolism disorder characterized by high blood levels of the amino acid phenylalanine. This results from a mutation in the gene responsible for phenylalanine hydroxylase, an enzyme that converts phenylalanine into tyrosine. When this enzyme is deficient, phenylalanine builds up in the blood, leading to symptoms such as vomiting, rashes, seizures, growth deficiency, and severe mental retardation. An early diagnosis and a diet restricting phenylalanine intake...
Biosynthesis of Nucleic Acids01:28

Biosynthesis of Nucleic Acids

Nucleic acid biosynthesis is a fundamental biochemical process that produces the purine and pyrimidine nucleotides essential for DNA and RNA synthesis. This pathway maintains a balanced nucleotide pool, preventing imbalances that could jeopardize genetic integrity and cellular function. Given the crucial role of nucleotides, their synthesis is tightly regulated to ensure proper cellular homeostasis.Purine BiosynthesisThe biosynthesis of purine nucleotides begins with ribose-5-phosphate, a...
Cofactors and Coenzymes01:24

Cofactors and Coenzymes

Enzymes are proteins made of amino acids. The functional group of each constituent amino acid catalyzes a wide variety of chemical reactions via ionic interactions or acid-base reactions. However, amino acids cannot catalyze oxidation-reduction and group transfer reactions and need to be aided by non-protein components called cofactors. Cofactors are also referred to as the chemical teeth of an enzyme.
Cofactors can be metallic ions or organic molecules called coenzymes. These types of helper...
Cofactors and Coenzymes01:27

Cofactors and Coenzymes

Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.

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Updated: Jun 27, 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

Cobalamin-dependent and cobamide-dependent methyltransferases.

Rowena G Matthews1, Markos Koutmos, Supratim Datta

  • 1Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109-2216, USA. rmatthew@umich.edu

Current Opinion in Structural Biology
|December 9, 2008
PubMed
Summary
This summary is machine-generated.

Methyltransferases using cobalamin cofactors are crucial for energy generation and methionine synthesis. Complex conformational changes in these enzymes are essential for their catalytic cycle involving labile intermediates.

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Last Updated: Jun 27, 2026

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

Published on: November 22, 2014

Antibody-Free Assay for RNA Methyltransferase Activity Analysis
08:31

Antibody-Free Assay for RNA Methyltransferase Activity Analysis

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In Vitro Assay to Measure Phosphatidylethanolamine Methyltransferase Activity
09:33

In Vitro Assay to Measure Phosphatidylethanolamine Methyltransferase Activity

Published on: January 5, 2016

Area of Science:

  • Biochemistry
  • Enzymology
  • Bioenergetics

Background:

  • Methyltransferases utilizing cobalamin (or cobamides) are key enzymes in biological methyl transfer.
  • These enzymes are vital for energy generation in anaerobic organisms and homocysteine to methionine conversion in diverse life forms.

Purpose of the Study:

  • To elucidate the complex conformational changes in methyltransferases during catalysis.
  • To understand the strategies employed by these enzymes to facilitate and control these dynamic structural rearrangements.

Main Methods:

  • Spectroscopic studies
  • Structural biology analyses
  • Enzyme kinetics

Main Results:

  • Identified specific conformational changes essential for the catalytic cycle of cobalamin-dependent methyltransferases.
  • Revealed the role of cobalt coordination and intermediate lability in driving these structural dynamics.

Conclusions:

  • Complex conformational changes are integral to the function of methyltransferases.
  • Understanding these dynamics provides insights into enzyme mechanisms and potential therapeutic targets.