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Information on EC 6.2.1.16 - acetoacetate-CoA ligase and Organism(s) Rattus norvegicus and UniProt Accession Q9JMI1
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6.2.1.16 acetoacetate-CoA ligaseIUBMB Comments
Also acts, more slowly, on L-3-hydroxybutanoate.
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Word Map
- 6.2.1.16
- ketone
- cholesterol
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lipogenesis
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body-utilizing
-
lipogenic
-
thiolase
- hmg-coa
- 3-hydroxybutyrate
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coa-transferase
- cholestyramine
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zoogloea
- ramigera
- srebp-2
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
acetoacetyl-coa synthetase, slaacs, acetoacetate-coa ligase, acetoacetyl coa synthetase, acetoacetyl-coa ligase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Acetoacetate--CoA ligase
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Acetoacetyl CoA synthetase
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Acetoacetyl-CoA ligase
Acetoacetyl-CoA synthase
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Acetoacetyl-CoA synthetase
Acetoacetyl-coenzyme A synthetase
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Synthetase, acetoacetyl coenzyme A
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Acetoacetyl-CoA ligase
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Acetoacetyl-CoA synthetase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acid-thiol ligation
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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
39394-62-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
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45% of the activity relative to acetoacetate
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?
ATP + acetoacetate + CoA
AMP + diphosphate + acetoacetyl-CoA
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-
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?
ATP + acetoacetate + CoA
AMP + diphosphate + acetoacetyl-CoA
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-
-
?
ATP + acetoacetate + CoA
AMP + diphosphate + acetoacetyl-CoA
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-
-
?
ATP + acetoacetate + CoA
AMP + diphosphate + acetoacetyl-CoA
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-
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-
?
ATP + acetoacetate + CoA
AMP + diphosphate + acetoacetyl-CoA
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no activity with GTP, UTP, CTP or ADP
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?
ATP + acetoacetate + CoA
AMP + diphosphate + acetoacetyl-CoA
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no activity with GTP and CTP
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-
?
ATP + L-3-hydroxybutanoate + CoA
AMP + diphosphate + L-3-hydroxybutyryl-CoA
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20% of the activity relative to acetoacetate
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-
?
ATP + L-3-hydroxybutanoate + CoA
AMP + diphosphate + L-3-hydroxybutyryl-CoA
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48% of the activity relative to acetoacetate
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-
?
additional information
?
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primary role of acetoacetate as a substrate in lipogenesis is to promote cholesterol biosynthesis. Regulation of acetoacetyl-CoA synthetase is synchronized with the regulation of cholesterol biosynthesis
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?
additional information
?
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enzyme normally functions in the re-utilization of some of the acetoacetate produced within the mitochondrion as well as that reaching the cytoplasm
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?
additional information
?
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AACS in adipose tissue plays an important role in utilizing ketone bodies for the fatty acid-synthesis during adipose tissue development
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
primary role of acetoacetate as a substrate in lipogenesis is to promote cholesterol biosynthesis. Regulation of acetoacetyl-CoA synthetase is synchronized with the regulation of cholesterol biosynthesis
-
-
?
additional information
?
-
-
enzyme normally functions in the re-utilization of some of the acetoacetate produced within the mitochondrion as well as that reaching the cytoplasm
-
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?
additional information
?
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AACS in adipose tissue plays an important role in utilizing ketone bodies for the fatty acid-synthesis during adipose tissue development
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
-
absolute requirement for a monovalent cation and a divalent cation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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in male rat liver, specific activity reaches a maximum at 4 weeks of age, then gradually decreases, in female rats, the maximum activity is reached at 6 weeks of age, and it is 3fold higher than in males
additional information
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streptozotocin-induced diabetes results in a decrease in acetoacetyl-CoA synthetase specific activity in rat liver, but not in other acetoacetyl-CoA synthetase containing tissues, e.g kidney, lung or brain, hepatic acetoacetyl-CoA synthetase activity is 8fold higher in rats fed with cholestyramine and pravastatin
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
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pH 6.0: about 30% of maximal activity, pH 9.0: about 65% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
expression of AACS mRNA in the cerebellum is restricted primarily to glial cells
in cerebral cortex expression of AACS mRNA is restricetd to neuronal cells
expression of AACS mRNA in the cerebellum is restricted primarily to glial cells
in cerebral cortex expression of AACS mRNA is restricetd to neuronal cells
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AACS mRNA is preferentially detected in mature adipocytes but not in preadipocytes. AACS mRNA expression in primary preadipocytes increases during the adipocyte differentiation
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diurnal variation of activity with the peak in the middle of the dark cycle. Activity level is higher in femals than in males
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AACS_RAT
672
0
75040
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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expression of a Streptomyces mevalonate pathway gene cluster starting from HMG-CoA synthase and including isopentenyl diphosphate isomerase, idi, type 2 gene and the yeast idi type 1 and rat acetoacetate-CoA ligase genes in Escherichia coli, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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, 0.1 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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ito, M.; Fukui, T.; Kamokari, M.; Saito, T.; Tomita, K.
Purification and characterization of acetoacetyl-CoA synthetase from rat liver
Biochim. Biophys. Acta
794
183-193
1984
Rattus norvegicus
Bergstrom, J.D.; Edmond, J.
Rat liver acetoacetyl-CoA synthetase
Methods Enzymol.
110
3-9
1985
Rattus norvegicus
Bergstrom, J.D.; Edmond, J.
A radiochemical assay for acetoacetyl-CoA synthetase
Anal. Biochem.
149
358-364
1985
Homo sapiens, Rattus norvegicus, Zoogloea ramigera, Zoogloea ramigera 1-16-M / ATCC 19623
Stern, J.R.
A role of acetoacetyl-CoA synthetase in acetoacetate Utilization by rat liver cell fractions
Biochem. Biophys. Res. Commun.
44
1001-1007
1971
Rattus norvegicus
Bergstrom, J.D.; Wong, G.A.; Edwards, P.A.; Edmond, J.
The regulation of acetoacetyl-CoA synthetase activity by modulators of cholesterol synthesis in vivo and the utilization of acetoacetate for cholesterogenesis
J. Biol. Chem.
259
14548-14553
1984
Rattus norvegicus
Sato, H.; Takahashi, N.; Nakamoto, M.; Ohgami, M.; Yamazaki, M.; Fukui, T.
Effects of streptozotocin-induced diabetes on acetoacetyl-CoA synthetase activity in rats
Biochem. Pharmacol.
63
1851-1855
2002
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Nakamoto, M.; Takahashi, N.; Iwahori, A.; Sato, H.; Fukui, T.
Effects of development on acetoacetyl-CoA synthetase biosynthesis in rat liver
Biol. Pharm. Bull.
22
981-983
1999
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Iwahori, A.; Takahashi, N.; Nakamoto, M.; Iwama, M.; Fukui, T.
cDNA-derived amino acid sequence of acetoacetyl-CoA synthetase from rat liver
FEBS LETT.
466
239-243
2000
Rattus norvegicus, Rattus sp.
Yamasaki, M.; Hasegawa, S.; Suzuki, H.; Hidai, K.; Saitoh, Y.; Fukui, T.
Acetoacetyl-CoA synthetase gene is abundant in rat adipose, and related with fatty acid synthesis in mature adipocytes
Biochem. Biophys. Res. Commun.
335
215-219
2005
Rattus norvegicus
Ohnuki, M.; Takahashi, N.; Yamasaki, M.; Fukui, T.
Different localization in rat brain of the novel cytosolic ketone body-utilizing enzyme, acetoacetyl-CoA synthetase, as compared to succinyl-CoA:3-oxoacid CoA-transferase
Biochim. Biophys. Acta
1729
147-153
2005
Rattus norvegicus (Q9JMI1)
Yamasaki, M.; Hasegawa, S.; Kitani, T.; Hidai, K.; Fukui, T.
Differential effects of obesity on acetoacetyl-CoA synthetase gene in rat adipose tissues
Eur. J. Lipid Sci. Technol.
109
617-622
2007
Rattus norvegicus
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