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Literature summary extracted from

  • Crosby, H.A.; Heiniger, E.K.; Harwood, C.S.; Escalante-Semerena, J.C.
    Reversible N(E)-lysine acetylation regulates the activity of acyl-CoA synthetases involved in anaerobic benzoate catabolism in Rhodopseudomonas palustris (2010), Mol. Microbiol., 76, 874-888.
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
6.2.1.25 Rhodopseudomonas palustris
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
6.2.1.25 additional information acetylation of residue Lys512 inactivates BadA, deacetylation reactivates BadA. Acetyltransferase RpPat modifies BadA, and also modifies acetyl-CoA synthetase. At least two deacetylases reactivate BadAAc. One is SrtN, a sirtuintype NAD+-dependent deacetylase, the other deacetylase is lysine deacetylase LdaA, an acetate-forming protein deacetylase. LdaA reactivates HbaAc and AliAAc in vitro Rhodopseudomonas palustris

Renatured (Commentary)

EC Number Renatured (Comment) Organism
6.2.1.25 acetylation of residue Lys512 inactivates BadA, deacetylation reactivates BadA Rhodopseudomonas palustris

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.2.1.25 ATP + benzoate + CoA
-
 Rhodopseudomonas palustris AMP + diphosphate + benzoyl-CoA
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.2.1.25 BadA
-
 Rhodopseudomonas palustris