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Literature summary for 6.2.1.16 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
Search for more literature for 6.2.1.16

Cloned(Commentary)

Cloned (Comment) Organism
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

Inhibitors Comment Organism Structure
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)

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

Organism

Organism UniProt Comment Textmining
Streptomyces lividans
-
 gene aacS
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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)

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

Synonyms

Synonyms Comment Organism
Acetoacetyl-CoA synthetase
-
 Streptomyces lividans
SlAacS
-
 Streptomyces lividans

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Streptomyces lividans

General Information

General Information Comment Organism
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