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Related Concept Videos

Phase II Reactions: Methylation Reactions01:17

Phase II Reactions: Methylation Reactions

161
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...
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Transfer RNA Synthesis02:36

Transfer RNA Synthesis

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One of the unique features of tRNA is the presence of modified bases. In some tRNAs, modified bases account for nearly 20% of the total bases in the molecule. Altogether, these unusual bases protect the tRNA from enzymatic degradation by RNases.
Each of these chemical modifications is carried by a specific enzyme, post-transcription. All of these enzymes have unique base and site-specificity. Methylation, the most common chemical modification, is carried by at least nine different enzymes, with...
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Disubstituted Cyclohexanes: cis-trans Isomerism02:37

Disubstituted Cyclohexanes: cis-trans Isomerism

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Depending upon the different spatial orientation of the substituents, the disubstituted cycloalkanes exhibit two types of stereoisomers. The cis isomers have the substituents on the same side of the ring, whereas the trans isomers have the substituents on the opposite sides. These stereoisomers exhibit different physical properties and cannot be interconverted without breaking the carbon-carbon bonds.
In cyclohexane, the substituents can occupy different positions generating distinct isomers....
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Translesion DNA Polymerases02:10

Translesion DNA Polymerases

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Translesion (TLS) polymerases rescue stalled DNA polymerases at sites of damaged bases by replacing the replicative polymerase and installing a nucleotide across the damaged site. Doing so, TLS allows additional time for the cell to repair the damage before resuming regular DNA replication.
TLS polymerases are found in all three domains of life - archaea, bacteria, and eukaryotes. Of the different classes of TLS polymerases, members of the Y family are fitted with specialized structures that...
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tRNA Activation02:26

tRNA Activation

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Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
19.1K
Eukaryotic RNA Polymerases00:58

Eukaryotic RNA Polymerases

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RNA Polymerase (RNAP) is conserved in all animals, with bacterial, archaeal, and eukaryotic RNAPs sharing significant sequence, structural, and functional similarities. Among the three eukaryotic RNAPs, RNA Polymerase II is most similar to bacterial RNAP in terms of both structural organization and folding topologies of the enzyme subunits. However, these similarities are not reflected in their mechanism of action.
All three eukaryotic RNAPs require specific transcription factors, of which the...
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Related Experiment Video

Updated: Jun 15, 2025

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

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Isofunctional but Structurally Different Methyltransferases for Dithiolopyrrolone Diversification.

Li Su, Eva M Huber1, Margaretha Westphalen2

  • 1Technical University of Munich, TUM School of Natural Sciences, Department of Bioscience, Center for Protein Assemblies, 85748, Garching, Germany.

Angewandte Chemie (International Ed. in English)
|August 26, 2024
PubMed
Summary

Researchers identified the XrdM enzyme, responsible for methylating xenorhabdin (XRD) in bacteria. This discovery sheds light on dithiolopyrrolone (DTP) biosynthesis and reveals convergent enzyme evolution.

Keywords:
biosynthesisdithiolopyrrolone natural productsenzyme catalysispost-NRPS methylationstructural biology

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An Engineered Split-TET2 Enzyme for Chemical-inducible DNA Hydroxymethylation and Epigenetic Remodeling
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Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays
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Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays
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Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Natural Product Biosynthesis

Background:

  • Dithiolopyrrolone (DTP) natural products exhibit significant antibacterial, antifungal, and anticancer properties.
  • Amide N-methylation of the DTP core is crucial for fine-tuning bioactivity, but the responsible enzymes are often uncharacterized.
  • Xenorhabdin (XRD) is a DTP natural product with potential therapeutic applications.

Purpose of the Study:

  • To identify the enzyme responsible for xenorhabdin (XRD) amide N-methylation in Xenorhabdus doucetiae.
  • To investigate the structural and functional relationship between XrdM and other DTP-related methyltransferases.
  • To expand the understanding of post-non-ribosomal peptide synthetase (NRPS) amide methylation in DTP biosynthesis.

Main Methods:

  • Gene identification and characterization of the XrdM methyltransferase.
  • X-ray crystallography to determine enzyme structures.
  • Enzyme activity assays and site-directed mutagenesis to probe function.
  • Bioinformatic analysis and comparative modeling.

Main Results:

  • The amide methyltransferase XrdM was identified as responsible for xenorhabdin (XRD) methylation in Xenorhabdus doucetiae.
  • XrdM is functionally similar to DtpM (involved in thiolutin biosynthesis) but possesses an unrelated X-ray structure.
  • The study reveals convergent evolution of two structurally distinct enzymes catalyzing the same methylation reaction.

Conclusions:

  • XrdM is a novel enzyme involved in DTP biosynthesis, expanding the known mechanisms of post-NRPS modification.
  • The findings highlight convergent evolution in enzyme function, with different structural solutions for the same biochemical reaction.
  • This research provides insights into the diversity of natural product biosynthesis and enzyme evolution.