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Literature summary extracted from

  • Hasegawa, S.; Yamasaki, M.; Fukui, T.
    Degradation of acetoacetyl-CoA synthetase, a ketone body-utilizing enzyme, by legumain in the mouse kidney (2014), Biochem. Biophys. Res. Commun., 453, 631-635 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.2.1.16 gene Aacs, cloning and recombinant expression of FLAG-tagged enzyme in Lenti-X-293T cells. AACS and legumain are transiently expressed in HEK-293 cells Mus musculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
6.2.1.16 cytosol
-
 Mus musculus 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.2.1.16 Mg2+ required Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.2.1.16 ATP + acetoacetate + CoA Mus musculus
-
 AMP + diphosphate + acetoacetyl-CoA
-
 ?
6.2.1.16 ATP + acetoacetate + CoA Mus musculus ddY
-
 AMP + diphosphate + acetoacetyl-CoA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.2.1.16 Mus musculus Q9D2R0
-
-
6.2.1.16 Mus musculus ddY Q9D2R0
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
6.2.1.16 proteolytic modification enzyme AACS is posttranslationally regulated, being cleaved at a specific site in the kidney. In vivo cleavage of enzyme AACS by legumain in HEK 293 cells generates the 55 kDa product from AACS. Incubation of recombinant AACS with recombinant legumain results in the degradation of AACS, optimally at pH 4.5. Knockdown of legumain with short-hairpin RNA against legumain using the hydrodynamics method leads to a decrease in the 55 kDa band of AACS in mouse kidney. Legumain is involved in the processing of AACS through the lysosomal degradation pathway in the kidney. Suppression of legumain results in a decrease in the cleaved form of AACS protein, and an increase in the full-length form of AACS protein. Legumain is involved in the cleavage of AACS in the kidney, suggesting that AACS is degraded by the lysosomal pathway Mus musculus

Purification (Commentary)

EC Number Purification (Comment) Organism
6.2.1.16 recombinant FLAG-tagged enzyme from Lenti-X-293T cells by affinity chromatography and ultrafiltration Mus musculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.2.1.16 adipocyte
-
 Mus musculus
-
6.2.1.16 kidney the short form of an AACS band is detected in the kidney Mus musculus
-
6.2.1.16 liver
-
 Mus musculus
-
6.2.1.16 additional information no expression in cerebrum, cerebellum, skeletal muscle, spleen, heart, and lung, expression analysis, overview Mus musculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.2.1.16 ATP + acetoacetate + CoA
-
 Mus musculus AMP + diphosphate + acetoacetyl-CoA
-
 ?
6.2.1.16 ATP + acetoacetate + CoA
-
 Mus musculus ddY AMP + diphosphate + acetoacetyl-CoA
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.2.1.16 AACS
-
 Mus musculus
6.2.1.16 Acetoacetyl-CoA synthetase
-
 Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
6.2.1.16 ATP
-
 Mus musculus

General Information

EC Number General Information Comment Organism
6.2.1.16 metabolism Legumain is involved in the cleavage of AACS in the kidney, suggesting that AACS is degraded by the lysosomal pathway Mus musculus
6.2.1.16 physiological function in the cytosol, acetoacetate is converted to acetoacetyl-CoA by acetoacetyl-CoA synthetase (AACS) for the synthesis of cholesterol and fatty acids. Acetoacetyl-CoA synthetase is a ketone body-utilizing enzyme, which is responsible for the synthesis of cholesterol and fatty acids from ketone bodies in lipogenic tissues, such as the liver and adipocytes. Enzyme AACS is posttranslationally regulated, being cleaved at a specific site in the kidney Mus musculus