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Information on EC 3.1.2.1 - acetyl-CoA hydrolase and Organism(s) Rattus norvegicus and UniProt Accession Q99NB7

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.2 Thioester hydrolases
                3.1.2.1 acetyl-CoA hydrolase
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This record set is specific for:
Rattus norvegicus
UNIPROT: Q99NB7 not found.
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The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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acetyl-CoA
+
H2O
=
CoA
+
acetate
+
=
+
Synonyms
acetyl-coa hydrolase, acot12, ach1p, human arylamine n-acetyltransferase type 1, acetyl coa hydrolase, (mouse)nat2, acetyl-coa decarbonylase synthase enzyme complex, mouse arylamine n-acetyltransferase type 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetyl-CoA hydrolase
-
Acetate utilization protein
-
-
-
-
acetyl coenzyme A acylase
-
-
-
-
acetyl coenzyme A deacylase
-
-
-
-
acetyl coenzyme A hydrolase
-
-
-
-
acetyl-CoA acylase
-
-
-
-
acetyl-CoA deacylase
-
-
-
-
acetyl-CoA hydrolase
-
-
-
-
hydrolase, acetyl coenzyme A
-
-
-
-
rACH
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + H2O = CoA + acetate
show the reaction diagram
the bifunctional enzyme is identical with a 3-ketoacyl-CoA thiolase isozyme, i.e. THL, EC 2.3.1.9, determined by internal peptide amino acid sequence comparison
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of thioester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA hydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9027-54-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
?
butanoyl-CoA + H2O
CoA + butanoate
show the reaction diagram
about 20% of the activity with acetyl-CoA
-
?
hexanoyl-CoA + H2O
CoA + hexanoate
show the reaction diagram
about 10% of the activity with acetyl-CoA
-
?
acetoacetyl-CoA
acetoacetate + CoA
show the reaction diagram
-
-
-
-
?
acetyl-CoA + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
butyryl-CoA + H2O
butanoate + CoA
show the reaction diagram
-
-
-
-
?
hexanoyl-CoA
hexanoate + CoA
show the reaction diagram
-
-
-
-
?
malonyl-CoA
malonate + CoA
show the reaction diagram
-
-
-
-
?
octanoyl-CoA
octanoate + CoA
show the reaction diagram
-
-
-
-
?
propionyl-CoA + H2O
CoA + propionate
show the reaction diagram
-
-
-
-
?
succinyl-CoA
succinate + CoA
show the reaction diagram
-
-
-
-
?
valeryl-CoA
pentanoate + CoA
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
substrate and chain-length specificity of the mitochondrial enzyme, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
-
activates
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-Butanedione
-
-
AMP
-
inhibits at 50 mM the stimulation of the enzyme by ATP
DL-lipoic acid
-
-
EDTA
-
enhances the inactivation of the enzyme in the presence of iron and L-ascorbic acid
Hydroxycitrate
-
-
L-ascorbic acid
-
inactivation of the purified enzyme by incubation at 37°C, enhancing by addition of Cu2+, Fe2+ and Fe3+
palmitoyl-CoA
-
-
Phenylglyoxal
-
-
phosphate
-
50% inhibition
Triton X-100
-
-
valeryl-CoA
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-thiadicarboxylic acid
-
activity increases
acetate
-
hydrolase increased 3fold by 100-250 mM acetate
acetyl-CoA
-
at time of rewarming 0.5 mM acetyl-CoA restores the activity about 50%
adenosine 5'-[beta,gamma-imido]triphosphate
-
with adoPP[CH2]P a 2.5fold activation of the cold-labile cytosolic enzyme at 2 mM, with adoPP[NH]P a 3.7fold activation respectively
albumin
-
albumin enhances the reactivation of the monomeric form
-
alpha-(p-chlorophenoxy)isobutyric acid
-
high activity of the enzyme for over 72h
bis(carboxymethylthio)-l,10 decane
-
rats fed a high-carbohydrate diet
CTP
-
counteracts the inhibition of the cold-labile cytosolic enzyme by ADP
cystamine
diacetylcystamine
-
activation
diphosphate
-
450 mM pyrophosphate restores the activity about 80% at time of rewarming
disulfide peptides
-
activation
-
dithiothreitol
-
oxidized, activation
DL-beta-hydroxy-butyrate
-
hydrolase increases 50-70% by 100 mM DL-beta-hydroxy-butyrate
ethyl chlorophenoxyisobutyrate
fluoroacetate
-
hydrolase increases 50-70% by 100 mM fluoroacetate
GSH
-
activation
GSSG
-
activation
NADH
-
stimulation
Oxytocin
-
activation
penicillamine disulfide
-
activation
phosphate
-
920 mM phosphate restores the activity about 80% at time of rewarming
pressinoic acid
-
activation
propionate
-
hydrolase increases 50-70% by 250 mM propionate
Somatostatin
-
like[tyr1]somatostatin and tyr-somatostatin the most potent activator
tetradecylthioacetic acid
-
activity increases
triiodothyronine
-
activity increases
Tyr-somatostatin
-
activation
Vasopressin
-
activation
[arg8]vasotocin
-
activation
[tyr1]somatostatin
-
activation
additional information
-
the enzyme is induced in mitochondria by di(2-ethylhexyl)phthalate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.153 - 0.22
acetyl-CoA
0.00006 - 15
acetyl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017
CoA
-
pH 7.4
0.0145
GDP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.3
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
-
activity enhanced at higher pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
37
-
warming at 37°C after cold exposure is optimal for reactivation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACO12_RAT
556
0
62018
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
124000
gel filtration
62000
2 * 62000, SDS-PAGE
62017
2 * 62017, calculation from nucleotide sequence
135000
136000
-
gel filtration, cytosolic native enzyme in the presence of 2 mM ATP, dimeric form
155000
-
gel filtration
157000
-
gel filtration, mitochondrial enzyme
160000
-
sedimentation velocity in a sucrose density gradient
240000
245000
-
gel filtration, cytosolic native enzyme in the presence of 2 mM ATP, tetrameric form
340000
-
equilibrium centrifugation
43000
-
x * 43000, SDS-PAGE
63000
-
2 * 63000, SDS-PAGE
64000
-
4 * 64000, SDS-PAGE
68000
-
SDS-PAGE gel electrophoresis, the cold labile cytosolic acetyl-CoA hydrolase
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
?
-
x * 43000, SDS-PAGE
dimer
monomer
-
sucrose density gradient centrifugation
tetramer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
-
purified dimeric enzyme fairly stable in potassium phosphate buffer of pH 7.0-8.0
94477
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
sulfhydryl compounds, glycerol and high ionic strength in the range of 0.2-0.4 mM enhances stability during purification
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
L-ascorbic acid and Cu2+, inactivation irreversible
-
94480
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4 months, 4°C
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
14000fold
-
27.2fold from liver mitochondria in a 5-step chromatographical procedure
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Sf9 cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ACOT12 mRNA and protein levels in rat primary hepatocytes decrease following treatment with insulin
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
from cold inactivation
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Robinson, J.B.; Mahan, D.E.; Koeppe, R.E.
Studies on rat brain acyl-coenzyme A hydrolase (short chain)
Biochem. Biophys. Res. Commun.
71
959-965
1976
Rattus norvegicus
Manually annotated by BRENDA team
Bernson, V.S.M.
Acetyl-CoA hydrolase; activity, regulation and physiological significance of the enzyme in brown adipose tissue from hamster
Eur. J. Biochem.
67
403-410
1976
Mesocricetus auratus, Rattus norvegicus
Manually annotated by BRENDA team
Grigat, K.P.; Koppe, K.; Seufert, C.D.; Sling, H.D.
Acetyl-coenzyme A deacylase activity in liver is not an artifact. Subcellular distribution and substrate specificity of acetyl-coenzyme A deacylase activities in rat liver
Biochem. J.
177
71-79
1979
Rattus norvegicus
Manually annotated by BRENDA team
Prass, R.L.; Isohashi, F.; Utter, M.F.
Purification and characterization of an extramitochondrial acetyl coenzyme A hydrolase from rat liver
J. Biol. Chem.
255
5215-5223
1980
Bos taurus, Cavia porcellus, Gallus gallus, Mesocricetus auratus, Platyrrhini, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Namboodiri, M.A.A.; Weller, J.L.; Klein, D.C.
Rapid and reversible activation of acetyl CoA hydrolase in intact pineal cells by disulfide exchange
Biochem. Biophys. Res. Commun.
96
188-195
1980
Rattus norvegicus
Manually annotated by BRENDA team
Namboodiri, M.A.A.; Favilla, J.T.; Klein, D.C.
Activation of pineal acetyl coenzyme A hydrolase by disulfide peptides
J. Biol. Chem.
257
10030-10032
1982
Rattus norvegicus
Manually annotated by BRENDA team
Isohashi, F.; Nakanishi, Y.; Sakamoto, Y.
Effects of nucleotides on a cold labile acetyl-CoA hydrolase from the supernatant fraction of rat liver
Biochemistry
22
584-590
1983
Rattus norvegicus
Manually annotated by BRENDA team
Isohashi, F.; Nakanishi, Y.; Sakamoto, Y.
Factors affecting the cold inactivation of an acetyl-coenzyme-A hydrolase purified from the supernatant fraction of rat liver
Eur. J. Biochem.
134
447-452
1983
Rattus norvegicus
Manually annotated by BRENDA team
Isohashi, F.; Nakanishi, Y.; Matsunaga, T.; Sakamoto, Y.
A cold-labile acetyl-coenzyme-A hydrolase from the supernatant fraction of rat liver. Reactivation and reconstitution of the active species from the inactive monomer
Eur. J. Biochem.
142
177-181
1984
Rattus norvegicus
Manually annotated by BRENDA team
Bronfman, M.; Leighton, F.
Carnitine acyltransferase and acyl-coenzyme A hydrolase activities in human liver. Quantitative analysis of their subcellular localization
Biochem. J.
224
721-730
1984
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Sling, H.D.; Rescher, C.
On the regulation of cold-labile cytosolic and of mitochondrial acetyl-CoA hydrolase in rat liver
Eur. J. Biochem.
147
111-117
1985
Rattus norvegicus
Manually annotated by BRENDA team
Nakanishi, Y.; Isohashi, F.; Matsunaga, T.; Sakamoto, Y.
Oxidative inactivation of an extramitochondrial acetyl-CoA hydrolase by autoxidation of L-ascorbic acid
Eur. J. Biochem.
152
337-342
1985
Rattus norvegicus
Manually annotated by BRENDA team
Matsunaga, T.; Isohashi, F.; Nakanishi, Y.; Sakamoto, Y.
Physiological changes in the activities of extramitochondrial acetyl-CoA hydrolase in the liver of rats under various metabolic conditions
Eur. J. Biochem.
152
331-336
1985
Rattus norvegicus
Manually annotated by BRENDA team
Nakanishi, Y.; Isohashi, F.; Ebisuno, S.; Sakamoto, Y.
Binding of nucleotides to an extramitochondrial acetyl-CoA hydrolase from rat liver
Biochemistry
27
4822-4826
1988
Rattus norvegicus
Manually annotated by BRENDA team
Chabtree, B.; Souter, M.J.; Anderson, S.E.
Evidence that the production of acetate in rat hepatocytes is a predominantly cytoplasmic process
Biochem. J.
257
673-678
1989
Rattus norvegicus
Manually annotated by BRENDA team
Garras, A.; Asiedu, D.K.; Berge, R.K.
Subcellular localisation and induction of NADH-sensitive acetyl-CoA hydrolase and propionyl-CoA hydrolase activities in rat liver under lipogenic conditions after treatment with sulfur-substituted fatty acids
Biochim. Biophys. Acta
1255
154-160
1995
Rattus norvegicus
Manually annotated by BRENDA team
Nakanishi, Y.; Okamoto, K.; Isohashi, F.
Effects of chronic administration of the peroxisome proliferator, clofibrate, on cytosolic acetyl-CoA hydrolase in rat liver
Biochem. Pharmacol.
45
1403-1407
1993
Rattus norvegicus
Manually annotated by BRENDA team
Hovik, R.; Brodal, B.; Bartlett, K.; Osmundsen, H.
Metabolism of acetyl-CoA by isolated peroxisomal fractions: formation of acetate and acetoacetyl-CoA
J. Lipid Res.
32
993-999
1991
Rattus norvegicus
Manually annotated by BRENDA team
Yamashita, H.; Kaneyuki, T.; Tagawa, K.
Production of acetate in the liver and its utilization in peripheral tissues
Biochim. Biophys. Acta
1532
79-87
2001
Rattus norvegicus
Manually annotated by BRENDA team
Suematsu, N.; Okamoto, K.; Shibata, K.; Nakanishi, Y.; Isohashi, F.
Molecular cloning and functional expression of rat liver cytosolic acetyl-CoA hydrolase
Eur. J. Biochem.
268
2700-2709
2001
Rattus norvegicus (Q99NB7)
Manually annotated by BRENDA team
Yamashita, H.; Itsuki, A.; Kimoto, M.; Hiemori, M.; Tsuji, H.
Acetate generation in rat liver mitochondria: acetyl-CoA hydrolase activity is demonstrated by 3-ketoacyl-CoA thiolase
Biochim. Biophys. Acta
1761
17-23
2006
Rattus norvegicus
Manually annotated by BRENDA team
Horibata, Y.; Ando, H.; Itoh, M.; Sugimoto, H.
Enzymatic and transcriptional regulation of the cytoplasmic acetyl-CoA hydrolase ACOT12
J. Lipid Res.
54
2049-2059
2013
Rattus norvegicus (Q99NB7), Mus musculus (Q9DBK0)
Manually annotated by BRENDA team
Ronowska, A.; Szutowicz, A.; Bielarczyk, H.; Gul-Hinc, S.; Klimaszewska-Lata, J.; Dys, A.; Zysk, M.; Jankowska-Kulawy, A.
The regulatory effects of acetyl-CoA distribution in the healthy and diseased brain
Front. Cell. Neurosci.
12
169
2018
Rattus norvegicus
Manually annotated by BRENDA team