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Related Concept Videos

tRNA Activation02:26

tRNA Activation

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...
tRNA Activation02:26

tRNA Activation

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...
RNA Structure01:19

RNA Structure

The basic structure of RNA consists of a string of ribonucleotides attached by phosphodiester bonds. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
Different Types of RNA Have the Same Basic Structure
There are three main types of ribonucleic acid (RNA) involved in protein synthesis: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). All three...
RNA Structure01:23

RNA Structure

Overview
The basic structure of RNA consists of a five-carbon sugar and one of four nitrogenous bases. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
Different Types of RNA Have the Same Basic Structure
There are three main types of ribonucleic acid (RNA): messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). All three RNA types consist of a...
Transfer RNA Synthesis02:36

Transfer RNA Synthesis

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...
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...

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Related Experiment Video

Updated: Jun 28, 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

Structure-function relationships in methionine adenosyltransferases.

G D Markham1, M A Pajares

  • 1Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, PA 19111, USA.

Cellular and Molecular Life Sciences : CMLS
|October 28, 2008
PubMed
Summary
This summary is machine-generated.

Methionine adenosyltransferases (MATs) synthesize S-adenosylmethionine, a key methyl donor. This review integrates structural data to explain MAT mechanisms, folding, and disease links, identifying research gaps.

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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

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Last Updated: Jun 28, 2026

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
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Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry (CCMS)
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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Methionine adenosyltransferases (MATs) are crucial enzymes synthesizing S-adenosylmethionine (SAM), the primary biological methyl donor.
  • High sequence conservation in MAT catalytic subunits across bacteria and eukarya highlights conserved residues vital for activity and oligomerization.
  • Existing structural data reveal variations in complexes with substrates and products, suggesting multiple reaction mechanisms.

Purpose of the Study:

  • To provide a consensus interpretation of MAT structure and function by analyzing available structural data.
  • To elucidate the folding pathways of the catalytic subunit and the role of intermediates in achieving the active conformation.
  • To connect MAT structure-function insights with pathological conditions arising from impaired enzyme activity and identify future research directions.

Main Methods:

  • Comprehensive analysis of existing structural data for Methionine adenosyltransferases (MATs).
  • Integration of folding studies to understand catalytic subunit formation and intermediate importance.
  • Comparative analysis of bacterial and eukaryotic MAT structures.

Main Results:

  • Consensus interpretation of MAT structure, activity, and oligomerization based on conserved residues.
  • Insights into the three-domain folding process and the significance of folding intermediates.
  • Correlation between structural features and pathological consequences of MAT dysfunction.

Conclusions:

  • Structural data provide a framework for understanding MAT mechanisms and their link to disease.
  • Further research is needed to clarify obscure aspects of MAT function and reaction pathways.
  • Understanding MATs is critical for addressing metabolic disorders linked to SAM synthesis.