Acetyl-CoA synthetase activity is enzymatically regulated by lysine acetylation using acetyl-CoA or acetyl-phosphate as donor molecule Article Swipe
Chuan Qin
,
Leonie G. Graf
,
Kilian Striska
,
Markus Janetzky
,
Norman Geist
,
Robin Specht
,
Sabrina Schulze
,
Gottfried J. Palm
,
Britta Girbardt
,
Babett Dörre
,
Leona Berndt
,
Stefan Kemnitz
,
Mark Doerr
,
Uwe T. Bornscheuer
,
Mihaela Delcea
,
Michael Lammers
·
YOU?
·
· 2024
· Open Access
·
· DOI: https://doi.org/10.1038/s41467-024-49952-0
YOU?
·
· 2024
· Open Access
·
· DOI: https://doi.org/10.1038/s41467-024-49952-0
The AMP-forming acetyl-CoA synthetase is regulated by lysine acetylation both in bacteria and eukaryotes. However, the underlying mechanism is poorly understood. The Bacillus subtilis acetyltransferase AcuA and the AMP-forming acetyl-CoA synthetase AcsA form an AcuA•AcsA complex, dissociating upon lysine acetylation of AcsA by AcuA. Crystal structures of AcsA from Chloroflexota bacterium in the apo form and in complex with acetyl-adenosine-5′-monophosphate (acetyl-AMP) support the flexible C-terminal domain adopting different conformations. AlphaFold2 predictions suggest binding of AcuA stabilizes AcsA in an undescribed conformation. We show the AcuA•AcsA complex dissociates upon acetyl-coenzyme A (acetyl-CoA) dependent acetylation of AcsA by AcuA. We discover an intrinsic phosphotransacetylase activity enabling AcuA•AcsA generating acetyl-CoA from acetyl-phosphate (AcP) and coenzyme A (CoA) used by AcuA to acetylate and inactivate AcsA. Here, we provide mechanistic insights into the regulation of AMP-forming acetyl-CoA synthetases by lysine acetylation and discover an intrinsic phosphotransacetylase allowing modulation of its activity based on AcP and CoA levels.
Related Topics
Concepts
Acetylation
Acetyl-CoA
Acetyltransferase
Lysine
Biochemistry
Bacillus subtilis
Coenzyme A
Cofactor
Transferase
Enzyme
Chemistry
Biology
Bacteria
Amino acid
Gene
Reductase
Genetics
Metadata
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1038/s41467-024-49952-0
- https://www.nature.com/articles/s41467-024-49952-0.pdf
- OA Status
- gold
- Cited By
- 15
- References
- 151
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4400741436
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
-
https://openalex.org/W4400741436Canonical identifier for this work in OpenAlex
- DOI
-
https://doi.org/10.1038/s41467-024-49952-0Digital Object Identifier
- Title
-
Acetyl-CoA synthetase activity is enzymatically regulated by lysine acetylation using acetyl-CoA or acetyl-phosphate as donor moleculeWork title
- Type
-
articleOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2024Year of publication
- Publication date
-
2024-07-17Full publication date if available
- Authors
-
Chuan Qin, Leonie G. Graf, Kilian Striska, Markus Janetzky, Norman Geist, Robin Specht, Sabrina Schulze, Gottfried J. Palm, Britta Girbardt, Babett Dörre, Leona Berndt, Stefan Kemnitz, Mark Doerr, Uwe T. Bornscheuer, Mihaela Delcea, Michael LammersList of authors in order
- Landing page
-
https://doi.org/10.1038/s41467-024-49952-0Publisher landing page
- PDF URL
-
https://www.nature.com/articles/s41467-024-49952-0.pdfDirect link to full text PDF
- Open access
-
YesWhether a free full text is available
- OA status
-
goldOpen access status per OpenAlex
- OA URL
-
https://www.nature.com/articles/s41467-024-49952-0.pdfDirect OA link when available
- Concepts
-
Acetylation, Acetyl-CoA, Acetyltransferase, Lysine, Biochemistry, Bacillus subtilis, Coenzyme A, Cofactor, Transferase, Enzyme, Chemistry, Biology, Bacteria, Amino acid, Gene, Reductase, GeneticsTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
15Total citation count in OpenAlex
- Citations by year (recent)
-
2025: 11, 2024: 4Per-year citation counts (last 5 years)
- References (count)
-
151Number of works referenced by this work
- Related works (count)
-
10Other works algorithmically related by OpenAlex
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