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Literature summary for 2.3.1.B34 extracted from

  • Tucker, A.C.; Escalante-Semerena, J.C.
    Acetoacetyl-CoA synthetase activity is controlled by a protein acetyltransferase with unique domain organization in Streptomyces lividans (2013), Mol. Microbiol., 87, 152-167.
    View publication on PubMedView publication on EuropePMC
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + [AacS]-L-Lys617 Streptomyces lividans substrate acetoacetyl-CoA synthase AACS. Acetylation occurs at active site residue Lys617 CoA + [AacS]-Nepsilon-acetyl-L-Lys617
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 ?
acetyl-CoA + [AacS]-L-Lys617 Streptomyces lividans TK24 substrate acetoacetyl-CoA synthase AACS. Acetylation occurs at active site residue Lys617 CoA + [AacS]-Nepsilon-acetyl-L-Lys617
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 ?

Organism

Organism UniProt Comment Textmining
Streptomyces lividans
-
-
-
Streptomyces lividans TK24
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + [AacS]-L-Lys617 substrate acetoacetyl-CoA synthase AACS. Acetylation occurs at active site residue Lys617 Streptomyces lividans CoA + [AacS]-Nepsilon-acetyl-L-Lys617
-
 ?
acetyl-CoA + [AacS]-L-Lys617 substrate acetoacetyl-CoA synthase AACS. Acetylation occurs at active site residue Lys617 Streptomyces lividans TK24 CoA + [AacS]-Nepsilon-acetyl-L-Lys617
-
 ?

Synonyms

Synonyms Comment Organism
PatA
-
 Streptomyces lividans
SSPG_01886
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 Streptomyces lividans

General Information

General Information Comment Organism
physiological function enzyme PatA acetylates acetoacetyl-CoA synthase AacS at the active-site residue Lys617 and acetylation inactivates AacS. Acetylated AacS is deacetylated by a sirtuin-type protein deacetylase Streptomyces lividans