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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.2.1.16 gene aacS, expression in Escherichia coli and complementation of a deficiency in atoDA, encoding acetyl-CoA:acetotacetate CoA transferase, EC 2.8.3.8, in Escherichia coli strain DELtaatoDA DELTAcobB DELTApka Streptomyces lividans

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.2.1.16 additional information Streptomyces lividans GCN5-typeN-acetyltransferase SlPatA acetylates the enzyme at the active-site residue Lys617, the acetylation inactivates the enzyme, overview. Acetylated SlAacS is deacetylated by a sirtuin-type protein deacetylase Streptomyces lividans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.B34 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
-
 ?
2.3.1.B34 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
-
 ?
6.2.1.16 ATP + acetoacetate + CoA Streptomyces lividans
-
 AMP + diphosphate + acetoacetyl-CoA
-
 ?
6.2.1.16 ATP + acetoacetate + CoA Streptomyces lividans TK24
-
 AMP + diphosphate + acetoacetyl-CoA
-
 ?
6.2.1.16 additional information Streptomyces lividans SlAacS is a bona fide acetoacetyl-CoA synthetase, an AMP-forming acyl-CoA synthetase ?
-
 ?
6.2.1.16 additional information Streptomyces lividans TK24 SlAacS is a bona fide acetoacetyl-CoA synthetase, an AMP-forming acyl-CoA synthetase ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.B34 Streptomyces lividans
-
-
-
2.3.1.B34 Streptomyces lividans TK24
-
-
-
6.2.1.16 Streptomyces lividans
-
 gene aacS
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
6.2.1.16 acetylation Streptomyces lividans GCN5-typeN-acetyltransferase SlPatA acetylates the enzyme at the active-site residue Lys617, the acetylation inactivates the enzyme, overview. Acetylated SlAacS is deacetylated by a sirtuin-type protein deacetylase. SlAacS acetylation/deacetylation may represent a conserved mechanism for regulation of acetoacetyl-CoA synthetase activity in all domains of life Streptomyces lividans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.B34 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
-
 ?
2.3.1.B34 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
-
 ?
6.2.1.16 ATP + acetoacetate + CoA
-
 Streptomyces lividans AMP + diphosphate + acetoacetyl-CoA
-
 ?
6.2.1.16 ATP + acetoacetate + CoA
-
 Streptomyces lividans TK24 AMP + diphosphate + acetoacetyl-CoA
-
 ?
6.2.1.16 additional information SlAacS is a bona fide acetoacetyl-CoA synthetase, an AMP-forming acyl-CoA synthetase Streptomyces lividans ?
-
 ?
6.2.1.16 additional information SlAacS is a bona fide acetoacetyl-CoA synthetase, an AMP-forming acyl-CoA synthetase Streptomyces lividans TK24 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.B34 PatA
-
 Streptomyces lividans
2.3.1.B34 SSPG_01886
-
 Streptomyces lividans
6.2.1.16 Acetoacetyl-CoA synthetase
-
 Streptomyces lividans
6.2.1.16 SlAacS
-
 Streptomyces lividans

Cofactor

EC Number Cofactor Comment Organism Structure
6.2.1.16 ATP
-
 Streptomyces lividans

General Information

EC Number General Information Comment Organism
2.3.1.B34 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
6.2.1.16 physiological function acetoacetyl-CoA synthetase activity is required for growth of Streptomyces lividans on acetoacetate and is controlled by a protein acetyltransferase with unique domain organization Streptomyces lividans