Information on EC 6.2.1.16 - acetoacetate-CoA ligase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
6.2.1.16
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RECOMMENDED NAME
GeneOntology No.
acetoacetate-CoA ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + acetoacetate + CoA = AMP + diphosphate + acetoacetyl-CoA
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Butanoate metabolism
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Valine, leucine and isoleucine degradation
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SYSTEMATIC NAME
IUBMB Comments
acetoacetate:CoA ligase (AMP-forming)
Also acts, more slowly, on L-3-hydroxybutanoate.
CAS REGISTRY NUMBER
COMMENTARY hide
39394-62-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
female, strain Sprague-Dawley
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-
Manually annotated by BRENDA team
strain Rm 11134
SwissProt
Manually annotated by BRENDA team
gene aacS
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-
Manually annotated by BRENDA team
strain 1-16-M, ATCC 19623
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-
Manually annotated by BRENDA team
strain 1-16-M, ATCC 19623
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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knockdown of AACS inhibits differentiation of 3T3-L1 cells and suppresses expression of the adipocyte markers, peroxisome proliferator-activated receptor gamma and CCAAT/enhancer binding protein alpha
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
show the reaction diagram
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45% of the activity relative to acetoacetate
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-
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ATP + acetoacetate + CoA
AMP + diphosphate + acetoacetyl-CoA
show the reaction diagram
ATP + L-3-hydroxybutanoate + CoA
AMP + diphosphate + L-3-hydroxybutyryl-CoA
show the reaction diagram
ATP + L-3-hydroxybutyrate + CoA
AMP + diphosphate + L-3-hydroxybutyryl-CoA
show the reaction diagram
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-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + acetoacetate + CoA
AMP + diphosphate + acetoacetyl-CoA
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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can replace Mg2+ in activation, 26% of the activation relative to Mg2+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
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5 mM, 70% inhibition
diphosphate
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10 mM, 70% inhibition
phosphate
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-
additional information
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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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Tris
-
stimulates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.008 - 0.3
acetoacetate
0.033 - 0.06
ATP
0.01 - 0.091
CoA
1.4
L(+)-3-hydroxybutyrate
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0.075
L-(+)-3-hydroxybutyrate
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20
L-3-hydroxybutyrate
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pH 8.4
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00424
22°C, pH 8.0
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.4
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8.4
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activation of acetoacetate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
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pH 6.0: about 30% of maximal activity, pH 9.0: about 65% of maximal activity
6.2 - 8.6
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about 65% of maximal activity at pH 6.2 and 8.6
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
in cerebral cortex expression of AACS mRNA is restricetd to neuronal cells
Manually annotated by BRENDA team
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low expression level
Manually annotated by BRENDA team
expression of AACS mRNA in the cerebellum is restricted primarily to glial cells
Manually annotated by BRENDA team
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very low expression level
Manually annotated by BRENDA team
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lactating
Manually annotated by BRENDA team
in cerebral cortex expression of AACS mRNA is restricetd to neuronal cells
Manually annotated by BRENDA team
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low expression level
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75143
x * 75143, deduced from DNA sequence
80000
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gel filtration
100000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 75143, deduced from DNA sequence
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
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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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
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1 d, 30% loss of activity, in absence of glycerol
30
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1 d, 70% loss of activity, in absence of glycerol
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
40% loss of activity on freezing and thawing without glycerol
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in presence of 10% glycerol the enzyme can be frozen and thawed ten times without loss of activity
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in presence of 5% glycerol the enzyme can be frozen and thawed five times without loss of activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.07 mg/ml enzyme, 10 mM Tris/HCl buffer, pH 7.5, 50% glycerol, 10 mM 2-mercaptoethanol, stable for at least 1 month
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-20°C, 0.1 mg/ml enzyme, 10 mM Tris-HCl, pH 7.5, 50% glycerol, 10 mM 2-mercaptoethanol, stable for at least 3 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by a method that includes His affinity resin chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AACS DNa and amino acid sequence determination and analysis, and promoter identification and cloning, the human AACS promoter is a peroxisome-proliferator-activated receptor gamm, PPARgamma, target gene, the nuclear receptor is recruited to the AACS promoter by direct interaction with stimulating protein-1, Sp-1
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DNA and amino acid sequence determination, expression in Escherichia coli JM109, the engineered strain utilizes acetoacetate and can synthesize carotenoids, e.g. alpha-humulene, effectively, overview
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expressed in Escherichia coli
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expression of a cDNA isolated from human carcinoma HepG2 in Escherichia coli
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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
peroxisome-proliferator-activated receptor gamm, PPARgamma, induces AACS and adipogenesis. A PPAR-responsive element, PPRE-independent mechanism might be involved in PPARgamma-mediated AACS gene expression. PPARgamma-dependent activation of the human AACS gene is mediated by the GC boxes
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the human AACS promoter is a PPARgamma target gene. Nuclear receptor PPARgamma is recruited to the AACS promoter by direct interaction with Sp1
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treatment of hepatocytes with U18666A results in the upregulation of AACS gene expression
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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