In Salmonella enterica, the sirtuin-dependent protein acylation/deacylation system (SDPADS) maintains energy homeostasis during growth on low concentrations of acetate (Q41766402)

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scientific article published on 24 February 2011

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English	In Salmonella enterica, the sirtuin-dependent protein acylation/deacylation system (SDPADS) maintains energy homeostasis during growth on low concentrations of acetate	scientific article published on 24 February 2011

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scholarly article

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Europe PubMed Central

PMC publication ID

9 October 2017

In Salmonella enterica, the sirtuin-dependent protein acylation/deacylation system (SDPADS) maintains energy homeostasis during growth on low concentrations of acetate (English)

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Europe PubMed Central

PMC publication ID

9 October 2017

Salmonella enterica

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3

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Europe PubMed Central

PMC publication ID

9 October 2017

author name string

Chi Ho Chan

1

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Europe PubMed Central

PMC publication ID

9 October 2017

Jane Garrity

2

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Europe PubMed Central

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9 October 2017

Jorge C Escalante-Semerena

4

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9 October 2017

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publication date

24 February 2011

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9 October 2017

Molecular Microbiology

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9 October 2017

80

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Europe PubMed Central

PMC publication ID

9 October 2017

1

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

168-183

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Europe PubMed Central

PMC publication ID

9 October 2017

Nε-lysine acetylation of a bacterial transcription factor inhibits Its DNA-binding activity

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Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase

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Reversible N epsilon-lysine acetylation regulates the activity of acyl-CoA synthetases involved in anaerobic benzoate catabolism in Rhodopseudomonas palustris.

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Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux

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Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli

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AinS quorum sensing regulates the Vibrio fischeri acetate switch

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N-lysine propionylation controls the activity of propionyl-CoA synthetase

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Dephospho-CoA kinase provides a rapid and sensitive radiochemical assay for coenzyme A and its thioesters

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Biochemical and Crystallographic Analysis of Substrate Binding and Conformational Changes in Acetyl-CoA Synthetase † , ‡

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Control of acetyl-coenzyme A synthetase (AcsA) activity by acetylation/deacetylation without NAD(+) involvement in Bacillus subtilis

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Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases

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Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2

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Acetate kinase: not just a bacterial enzyme

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The beta-oxidation systems of Escherichia coli and Salmonella enterica are not functionally equivalent

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Acetyl-coenzyme A synthetase (AMP forming).

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Identification of the protein acetyltransferase (Pat) enzyme that acetylates acetyl-CoA synthetase in Salmonella enterica

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The Sir2 family of protein deacetylases

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Sirtuins: Sir2-related NAD-dependent protein deacetylases

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A link between transcription and intermediary metabolism: a role for Sir2 in the control of acetyl-coenzyme A synthetase

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Structure and Substrate Binding Properties of cobB, a Sir2 Homolog Protein Deacetylase from Escherichia coli

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Crystalline inorganic pyrophosphatase isolated from baker's yeast

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Lysogeny at mid-twentieth century: P1, P2, and other experimental systems

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Modulation of CRP-dependent transcription at the Escherichia coli acsP2 promoter by nucleoprotein complexes: anti-activation by the nucleoid proteins FIS and IHF.

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Cyclic AMP receptor protein-dependent activation of the Escherichia coli acsP2 promoter by a synergistic class III mechanism

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Role of Feedback Regulation of Pantothenate Kinase (CoaA) in Control of Coenzyme A Levels in Escherichia coli

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Short-chain fatty acid activation by acyl-coenzyme A synthetases requires SIR2 protein function in Salmonella enterica and Saccharomyces cerevisiae

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Regulation of coenzyme A biosynthesis

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Identifiers

10.1111/J.1365-2958.2011.07566.X

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

ResearchGate publication ID

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