ArticleThe Journal of biological chemistry2017
Cyclic AMP Inhibits the Activity and Promotes the Acetylation of Acetyl-CoA Synthetase through Competitive Binding to the ATP/AMP Pocket.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Enzymatic synthesis of azide by a promiscuous N-nitrosylase.Nature chemistry · 2024Article
- iTRAQ-Based Proteomic Profiling of Skin Aging Protective Effects ofMolecules (Basel, Switzerland) · 2024Article
- Acetyl-CoA synthetase activity is enzymatically regulated by lysine acetylation using acetyl-CoA or acetyl-phosphate as donor molecule.Nature communications · 2024Article
- Resveratrol production of a recombinantBiotechnology notes (Amsterdam, Netherlands) · 2022Article
- Protein Acetyltransferases Mediate Bacterial Adaptation to a Diverse Environment.Journal of bacteriology · 2021Review
- Post-translational Lysine Ac(et)ylation in Bacteria: A Biochemical, Structural, and Synthetic Biological Perspective.Frontiers in microbiology · 2021Review
- Bacterial Sirtuins Overview: An Open Niche to Explore.Frontiers in microbiology · 2021Review
- Proteomic and Transcriptomic Profiling Identifies Early Developmentally Regulated Proteins inCells · 2019Article
- Protein Acetylation in Bacteria.Annual review of microbiology · 2019Review
- Dynamic Expression Profile, Regulatory Mechanism and Correlation with Egg-laying Performance of ACSF Gene Family in Chicken (Gallus gallus).Scientific reports · 2018Article
- Identification of Key Residues for Enzymatic Carboxylate Reduction.Frontiers in microbiology · 2018Article
- Identification and characterization of two types of amino acid-regulated acetyltransferases in actinobacteria.Bioscience reports · 2017Article
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The high-affinity biosynthetic pathway for converting acetate to acetyl-coenzyme A (acetyl-CoA) is catalyzed by the central metabolic enzyme acetyl-coenzyme A synthetase (Acs), which is finely regulated both at the transcriptional level via cyclic AMP (cAMP)-driven trans-activation and at the post-translational level via acetylation inhibition. In this study, we discovered that cAMP directly binds to Salmonella enterica Acs (SeAcs) and inhibits its activity in a substrate-competitive manner. In addition, cAMP binding increases SeAcs acetylation by simultaneously promoting Pat-dependent acetylation and inhibiting CobB-dependent deacetylation, resulting in enhanced SeAcs inhibition. A crystal structure study and site-directed mutagenesis analyses confirmed that cAMP binds to the ATP/AMP pocket of SeAcs, and restrains SeAcs in an open conformation. The cAMP contact residues are well conserved from prokaryotes to eukaryotes, suggesting a general regulatory mechanism of cAMP on Acs.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.