Thiamine diphosphate adenylyl transferase from E. coli: functional characterization of the enzyme synthesizing adenosine thiamine triphosphate
2007
Characterizing an Enzyme that Makes a New Thiamine Compound in E. coli
publication
Evidence: moderate
Author Information
Author(s): Makarchikov Alexander F, Brans Alain, Bettendorff Lucien
Primary Institution: Center for Cellular and Molecular Neurobiology, University of Liège
Hypothesis
AThTP may be a signal produced in response to carbon starvation.
Conclusion
This study demonstrates the existence of an enzyme that synthesizes AThTP from ThDP and ADP or ATP.
Supporting Evidence
- AThTP is synthesized in E. coli only when there is no carbon source available.
- The enzyme requires divalent metal ions like Mn2+ or Mg2+ for activity.
- The enzyme has a pH optimum of 6.5–7.0 and a high Km for ThDP, indicating its activity depends on ThDP concentration.
Takeaway
Scientists found a new compound in bacteria that helps them respond to hunger, and they discovered the enzyme that makes it.
Methodology
The enzyme was partially purified from E. coli extracts and characterized for its functional properties and substrate specificity.
Limitations
The enzyme's activity was low and sensitive to purification methods, which may affect its stability.
Digital Object Identifier (DOI)
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