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Literature summary for 6.2.1.1 extracted from

  • Starai, V.J.; Celic, I.; Cole, R.N.; Boeke, J.D.; Escalante-Semerena, J.C.
    Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine (2002), Science, 298, 2390-2392.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
CobB Sir2 protein activation of the acetylated enzyme requires the nicotinamide adenine dinucleotide-dependent protein deacetylase activity of the CobB Sir2 protein Salmonella enterica

Organism

Organism UniProt Comment Textmining
Salmonella enterica
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
acetylation posttranslational regulation by acetylation of Lys609. Acetylation blocks synthesis of the adenylate intermediate but does not affect the thioester-forming activity of the enzyme Salmonella enterica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + acetate + CoA
-
Salmonella enterica AMP + diphosphate + acetyl-CoA
-
?

Synonyms

Synonyms Comment Organism
ACS
-
Salmonella enterica