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Diphtheria Toxin Catalytic Domain-Mediated Inhibition of Protein Synthesis
- Molecular classification
- Enzyme, ADP-ribosyltransferase, Toxin
01
Overview
The diphtheria toxin (DT) catalytic domain (Fragment A) is a potent enzyme that inhibits protein synthesis in eukaryotic cells. It functions as an NAD+-dependent ADP-ribosyltransferase, catalyzing the transfer of an ADP-ribose moiety from NAD+ to elongation factor 2 (EF-2). This modification inactivates EF-2, halting protein synthesis and leading to cell death. While not a therapeutic target itself, its mechanism of action is crucial for understanding diphtheria pathogenesis, and it has been exploited in the development of targeted therapies using chimeric toxins.
- Other names
- Diphtheria toxin catalytic domainFragment ANAD+-dependent ADP-ribosyltransferase (Diphtheria toxin)
02
Mechanism of action
NAD+-dependent ADP-ribosylation of elongation factor 2 (EF-2), leading to inhibition of protein synthesis.
03
Biological functions
Enzymatic inhibition of host-cell protein synthesisADP-ribosylation of EF-2Inhibition of translationCell death
04
Disease associations
InfectionDiphtheria
05
Safety considerations
High toxicityPotential for off-target effects in chimeric toxin therapies
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