Reversible N epsilon-lysine acetylation regulates the activity of acyl-CoA synthetases involved in anaerobic benzoate catabolism in Rhodopseudomonas palustris. (Q34033583)

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

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29 January 2020

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

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29 January 2020

cyclohexane-1-carbonyl-CoA

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ChEBI release 2020-05-28

Rhodopseudomonas palustris

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Rhodopseudomonas palustris

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29 January 2020

Erin K Heiniger

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29 January 2020

Caroline S. Harwood

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Caroline S Harwood

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29 January 2020

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Jorge C Escalante-Semerena

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16 March 2010

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29 January 2020

Molecular Microbiology

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29 January 2020

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29 January 2020

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29 January 2020

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29 January 2020

Anaerobic catabolism of aromatic compounds: a genetic and genomic view.

1 reference

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In Bacillus subtilis, the sirtuin protein deacetylase, encoded by the srtN gene (formerly yhdZ), and functions encoded by the acuABC genes control the activity of acetyl coenzyme A synthetase

1 reference

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1 reference

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Anaerobic metabolism of aromatic compounds

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Biochemical and structural characterization of the paralogous benzoate CoA ligases from Burkholderia xenovorans LB400: defining the entry point into the novel benzoate oxidation (box) pathway

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

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Structure and functions of the GNAT superfamily of acetyltransferases

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New enzymes involved in aerobic benzoate metabolism in Azoarcus evansii

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

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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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Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine

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https://pubmed.ncbi.nlm.nih.gov/20345662

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10.1111/J.1365-2958.2010.07127.X

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29 January 2020

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