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Literature summary for 6.2.1.16 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)

Cloned (Comment) Organism
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

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Mus musculus

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Mus musculus Q9D2R0
-
-
Mus musculus ddY Q9D2R0
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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)

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

Source Tissue

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
AACS
-
Mus musculus
Acetoacetyl-CoA synthetase
-
Mus musculus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Mus musculus

General Information

General Information Comment Organism
metabolism Legumain is involved in the cleavage of AACS in the kidney, suggesting that AACS is degraded by the lysosomal pathway Mus musculus
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