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Information on EC 3.1.2.20 - acyl-CoA hydrolase and Organism(s) Rattus norvegicus and UniProt Accession Q8VHK0
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EC Tree
3.1.2.20 acyl-CoA hydrolaseIUBMB Comments
Broad specificity for medium- to long-chain acyl-CoA. Insensitive to NAD+ (cf. EC 3.1.2.19 ADP-dependent medium-chain-acyl-CoA hydrolase)
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Word Map
- 3.1.2.20
- acyl-coas
- palmitoyl-coa
-
3.1.2.2
-
acyl-coa:cholesterol
- coash
- oleoyl-coa
-
teiis
-
hotdog-fold
-
acots
- arachidonoyl-coa
- degradation
- decanoyl-coa
- biotechnology
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
acyl-coa hydrolase, them2, type ii thioesterase, them1, acot11, them4, acot13, thioesterase superfamily member 2, te ii, thioesterase 2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACH1
-
-
-
-
ACH2
-
-
-
-
ACT
-
-
-
-
acyl CoA hydrolase
-
-
-
-
acyl coenzyme A hydrolase
-
-
-
-
acyl coenzyme A thioesterase
-
-
-
-
acyl-CoA thioesterase
brain acyl-CoA hydrolase
-
-
-
-
fatty acyl thioesterase I
-
-
-
-
HIV-Nef associated acyl coA thioesterase
-
-
-
-
hydrolase, acyl coenzyme A
-
-
-
-
hydrolase, palmitoyl coenzyme A
-
-
-
-
LACH1
-
-
-
-
LACH2
-
-
-
-
long chain acyl-CoA hydrolase
-
-
-
-
long chain acyl-CoA thioesterase
-
-
-
-
long chain fatty-acyl-CoA hydrolase
-
-
-
-
long chain fatty-acyl-CoA thioesterase
-
-
-
-
mitochondrial acyl-CoA thioesterase
-
-
-
-
palmitoyl coenzyme A hydrolase
-
-
-
-
palmitoyl thioesterase
-
-
-
-
palmitoyl-CoA deacylase
-
-
-
-
palmitoyl-CoA hydrolase
palmityl coenzyme A deacylase
-
-
-
-
palmityl thioesterase
-
-
-
-
palmityl thioesterase I
-
-
-
-
palmityl thioesterase II
-
-
-
-
TE
-
-
-
-
TE-II
-
-
-
-
thioesterase B
-
-
-
-
thioesterase II
-
-
-
-
very long chain acyl-CoA thioesterase
-
-
-
-
ZAP128
-
-
-
-
acyl-CoA thioesterase
-
-
-
-
palmitoyl-CoA hydrolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of thioester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA hydrolase
Broad specificity for medium- to long-chain acyl-CoA. Insensitive to NAD+ (cf. EC 3.1.2.19 ADP-dependent medium-chain-acyl-CoA hydrolase)
CAS REGISTRY NUMBER
COMMENTARY
37270-64-7
EC 3.1.2.2
9025-87-0
EC 3.1.2.20
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
2-nitrophenyl acetate + H2O
2-nitrophenol + acetate
synthetic substrate
-
-
?
acetoacetyl-CoA + H2O
CoA + acetoacetate
-
8% activity compared to palmitoyl-CoA
-
?
oleoyl-CoA + H2O
CoA + oleate
-
-
-
-
?
palmitoyl-CoA + H2O
CoA + palmitate
-
-
80783, 80785, 80791, 94478, 171023, 646115, 646125, 646128, 646129, 646131, 646134, 646140, 646141, 646144, 646162, 646164, 646167, 646169, 646171, 646173
-
-
?
tetradecylthioacetyl-CoA + H2O
CoA + tetradecylthioacetate
-
best substrate
-
-
?
4,8-dimethylnonanoyl-CoA + H2O
CoA + 4,8-dimethylnonanoate
-
-
?
4,8-dimethylnonanoyl-CoA + H2O
CoA + 4,8-dimethylnonanoate
involved in pristanic acid beta-oxidation, scheme of the pathway
-
?
4,8-dimethylnonanoyl-CoA + H2O
CoA + 4,8-dimethylnonanoate
hydrolysis allows transport of 4,8-dimethylnonanoate from peroxisomes to mitochondria for full oxidation
-
?
acyl-CoA + H2O
CoA + a carboxylate
-
long-chain to very-long-chain acyl-CoA
-
?
acyl-CoA + H2O
CoA + a carboxylate
-
broad specificity for medium-chain to long-chain acyl-CoA
-
?
acyl-CoA + H2O
CoA + a carboxylate
-
broad specificity for medium-chain to long-chain acyl-CoA
-
?
acyl-CoA + H2O
CoA + a carboxylate
-
saturated and unsaturated acyl-CoA
-
?
acyl-CoA + H2O
CoA + a carboxylate
-
long-chain fatty-acyl-CoA
-
-
?
acyl-CoA + H2O
CoA + a carboxylate
-
specific for acyl-CoA, S-palmitoyl-glutathione and S-palmitoyl-cysteine are no substrates
-
?
arachidonoyl-CoA + H2O
CoA + arachidonate
-
i.e. all-cis-5,8,11,14-eicosatetranoate
-
-
?
arachidonoyl-CoA + H2O
CoA + arachidonate
-
enzyme is responsible for the mobilization of stored arachidonic acid in cells
-
?
arachidonoyl-CoA + H2O
CoA + arachidonate
-
regulation, e.g. in the heart, of the enzyme is performed via beta-adrenergic receptors and their antagonists, e.g. actinomycin D
-
?
dodecanoyl-CoA + H2O
CoA + dodecanoate
-
i.e. lauroyl-CoA
-
-
?
hexadecanoyl-CoA + H2O
CoA + hexadecanoate
-
best substrate
-
-
?
hexadecanoyl-CoA + H2O
CoA + hexadecanoate
-
i.e. palmitoyl-CoA
-
-
?
hexadecanoyl-CoA + H2O
CoA + hexadecanoate
-
i.e. palmitoyl-CoA
-
-
?
hexadecanoyl-CoA + H2O
CoA + hexadecanoate
-
i.e. palmitoyl-CoA
-
-
?
octadecanoyl-CoA + H2O
CoA + octadecanoate
-
i.e. stearoyl-CoA
-
-
?
tetradecanoyl-CoA + H2O
CoA + tetradecanoate
-
i.e. myristoyl-CoA
-
-
?
tetradecanoyl-CoA + H2O
CoA + tetradecanoate
i.e. myristoyl-CoA
-
-
?
tetradecanoyl-CoA + H2O
CoA + tetradecanoate
-
i.e. myristoyl-CoA
-
-
?
tetradecanoyl-CoA + H2O
CoA + tetradecanoate
i.e. myristoyl-CoA
-
-
?
additional information
?
-
-
no activity with malonyl-CoA, ligneceroyl-CoA, and nervonoyl-CoA
-
-
?
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
palmitoyl-CoA + H2O
CoA + palmitate
-
-
80783, 80785, 80791, 94478, 171023, 646115, 646125, 646128, 646129, 646131, 646134, 646140, 646141, 646144, 646162, 646164, 646167, 646169, 646171, 646173
-
-
?
4,8-dimethylnonanoyl-CoA + H2O
CoA + 4,8-dimethylnonanoate
involved in pristanic acid beta-oxidation, scheme of the pathway
-
?
4,8-dimethylnonanoyl-CoA + H2O
CoA + 4,8-dimethylnonanoate
hydrolysis allows transport of 4,8-dimethylnonanoate from peroxisomes to mitochondria for full oxidation
-
?
arachidonoyl-CoA + H2O
CoA + arachidonate
-
enzyme is responsible for the mobilization of stored arachidonic acid in cells
-
?
arachidonoyl-CoA + H2O
CoA + arachidonate
-
regulation, e.g. in the heart, of the enzyme is performed via beta-adrenergic receptors and their antagonists, e.g. actinomycin D
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-acyl-sn-glycerol-3-phosphocholine
-
competitive inhibition at low concentration of palmitoyl-CoA
2,2'-(decane-1,10-diyldisulfanediyl)diacetic acid
-
palmitoyl-CoA hydrolase activity, L-fraction and peroxisomes, especially of 3-thia fatty acids treated rats
2,4-dichlorophenoxyacetate
-
reduced activity in microsomes and mitochondria
EDTA
-
inhibits the activity of the mitochondrial enzyme at concentrations of 0.5 mM
additional information
-
no inhibition by NEM, iodoacetamide, L-carnitine
-
Mg2+
-
inhibits the microsomal enzyme, at higher concentrations also the mitochondrial enzyme
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(tetradecylsulfanyl)acetic acid
-
stimulates palmitoyl-CoA, tetradecylthioacetyl-CoA and tetradecylthiopropionyl-CoA hydrolase activities in cytosol, mitochondrion and peroxisome, overview
3-(tetradecylsulfanyl)propanoic acid
-
stimulates palmitoyl-CoA, tetradecylthioacetyl-CoA and tetradecylthiopropionyl-CoA hydrolase activities in cytosol, mitochondrion and peroxisome, overview
FAD
-
stimulates the activity of the mitochondrial-matrix enzyme up to 0.4 mM
fish oil
-
partially hydrogenated, hydrolase activity reaches maximum after administration of the dietary oil for 6.5 days
-
isoproterenol
-
stimulates enzyme expression, can be blocked by specific beta-adrenoreceptor antagonists, e.g. actinomycin D
di(2-ethylhexyl)phthalate
strong induction in liver, moderately in kidney
di(2-ethylhexyl)phthalate
induction in liver, slightly in kidney
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.003 - 0.009
-
partially purified enzyme, medium- and long chain fatty acid hydrolase activity
additional information
additional information
-
activities in different subcellular fractions with different substrates after induction with 3-thia fatty acids, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
WY-14643 causes a significant induction of cte1 in isolated adult rat cardiomyocytes
additional information
-
-
80783, 80785, 80787, 80791, 94478, 171023, 646115, 646118, 646121, 646128, 646129, 646134, 646137, 646138, 646140, 646141, 646144, 646150, 646151, 646155, 646157
-
of rats treated with 3-thia fatty acids, i.e. tetradecylthioacetic acid and 3-dithiacarboxylic acid
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
-
-
-
-
80783, 80785, 80791, 171023, 646115, 646121, 646129, 646134, 646135, 646137, 646141, 646144, 646150, 646155, 646157
-
-
80783, 80787, 80791, 94478, 646115, 646121, 646125, 646128, 646131, 646138, 646140, 646144, 646150, 646151, 646155, 646158, 646162, 646163
-
-
additional information
-
substrate specificities in different subcellular fractions
-
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). ACOT8_RAT
320
0
36003
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
130000
-
gel filtration, glycerol is included in the eluting buffer
19000
35000 - 50000
-
different long-chain to very-long-chain acyl-CoA thioesterases from mitochondrial and cytosolic fractions, gel filtration
40000
40900
45000
59000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
tetramer
trimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, partially purified enzyme, at least 1 month without loss of activity
-
-70°C, pure enzyme, 0.1 M potassium phosphate, pH 7.5, 30% v/v ethylene glycol, loss of 50% activity within 5 days
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial purification of the 4,8-dimethylnonanoyl-CoA hydrolysing enzyme from liver peroxisomes
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, expression in Escherichia coli fused to maltose-binding protein
DNA and amino acid sequence determination and analysis, expression in CHO cells
DNA sequence determination and analysis, subcloning in Escherichia coli, and expression in CHO cells
expression of cDNA in chinese hamster ovary cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
very low in preadipocyte, after differentiation 18-fold increase, further enhanced by treatment with lipids or troglitazone
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Berge, R.K.; Dossland, B.
Differences between microsomal and mitochondrial-matrix palmitoyl-coenzyme A hydrolase, and palmitoyl-L-carnitine hydrolase from rat liver
Biochem. J.
181
119-125
1979
Rattus norvegicus
Mentlein, R.; Suttorp, M.; Heymann, E.
Specificity of purified monoacylglycerol lipase, palmitoyl-CoA hydrolase, palmitoyl-carnitine hydrolase, and nonspecific carboxylesterase from rat liver microsomes
Arch. Biochem. Biophys.
228
230-246
1984
Rattus norvegicus
Mentlein, R.; Rix-Matzen, H.; Heymann, E.
Subcellular localization of non-specific carboxylesterases, acylcarnitine hydrolase, monoacylglycerol lipase and palmitoyl-CoA hydrolase in rat liver
Biochim. Biophys. Acta
964
319-328
1988
Rattus norvegicus
Berge, R.K.; Farstad, M.
Dual localization of long-chain acyl-CoA hydrolase in rat liver: one in the microsomes and one in the mitochondrial matrix
Eur. J. Biochem.
95
89-97
1979
Rattus norvegicus
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
Mukherjee, J.J.; Jay, F.T.; Choy, P.C.
Purification, characterization and modulation of a microsomal carboxylesterase in rat liver for the hydrolysis of acyl-CoA
Biochem. J.
295
81-86
1993
Rattus norvegicus
Alexson, S.E.H.; Svensson, L.T.; Nedergaard, J.
NADH-sensitive propionyl-CoA hydrolase in brown adipose tissue mitochondria of the rat
Biochim. Biophys. Acta
1005
13-19
1989
Rattus norvegicus
Wilcke, M.; Alexson, S.E.H.
Characterization of acyl-CoA thioesterase activity in isolated rat liver peroxisomes. Partial purification and characterization of a long-chain acyl-CoA thioesterase
Eur. J. Biochem.
222
803-811
1994
Rattus norvegicus
Srere, P.A.; Seubert, W.; Lynen, F.
Palmityl coenzyme A deacylase
Biochim. Biophys. Acta
33
313-318
1959
Rattus norvegicus, Sus scrofa
Kurooka, S.; Hosoki, K.; Yoshimura, Y.
Some properties of long fatty acyl-coenzyme A thioesterase in rat organs
J. Biochem.
71
625-634
1972
Rattus norvegicus
Bonser, R.W.; Lunt, G.G.
The long-chain fatty acyl-coenzyme A hydrolase activity of rat cerebral cortex
Biochem. Soc. Trans.
4
321-324
1976
Rattus norvegicus
Berge, R.K.; Farstad, M.
Purification and characterization of long-chain acyl-CoA hydrolase from rat liver mitochondria
Eur. J. Biochem.
96
393-401
1979
Rattus norvegicus
Berge, R.K.
Purification and characterization of a long-chain acyl-CoA hydrolase from rat liver microsomes
Biochim. Biophys. Acta
574
321-333
1979
Rattus norvegicus
Knauer, T.E.
Factors affecting the activity and stability of the palmitoyl-coenzyme A hydrolase of rat brain
Biochem. J.
179
515-523
1979
Rattus norvegicus
Hagen, L.E.; Berge, R.R.; Bakken, A.; Farstad, M.
Effects of ethanol and protein dilution on microsomal palmitoyl-CoA hydrolase activity assayed by different methods
FEBS Lett.
110
205-208
1980
Rattus norvegicus
Knauer, T.E.; Gureck, J.J.; Knauer, G.R.
Substrate stabilization of the palmitoyl-coenzyme A hydrolase activity of rat submaxillary gland
Biochem. J.
187
269-272
1980
Rattus norvegicus
Berge R.K.
Physiochemical properties of the long-chain-acyl-CoA hydrolase from rat liver microsomes
Eur. J. Biochem.
111
67-72
1980
Rattus norvegicus
Miyazawa, S.; Furuta, S.; Hashimoto, T.
Induction of a novel long-chain acyl-CoA hydrolase in rat liver by administration of peroxisome proliferators
Eur. J. Biochem.
117
425-430
1981
Rattus norvegicus
Berge, R.K.; Farstad, M.
Long-chain fatty acyl-CoA hydrolase from rat liver mitochondria
Methods Enzymol.
71
234-242
1981
Rattus norvegicus
Berge, R.K.; Slinde, E.; Farstad, M.
Variations in the activity of microsomal palmitoyl-CoA hydrolase in mixed micelle solutions of palmitoyl-CoA and non-ionic detergents of the Triton X series
Biochim. Biophys. Acta
666
25-35
1981
Rattus norvegicus
Berge, R.K.; Bakke, O.M.; Farstad, M.; Aarsland, A.
Subcellular distributions of lipid-metabolizing enzymes in rat liver after treatment with tiadenol, clofibrate and phenobarbital
Biochem. Soc. Trans.
9
576
1981
Rattus norvegicus
-
Mentlein, R.; Berge, R.K.; Heymann, E.
Identity of purified monoacylglycerol lipase, palmitoyl-CoA hydrolase and aspirin-metabolizing carboxylesterase from rat liver microsomal fractions. A comparative study with enzymes purified in different laboratories
Biochem. J.
232
479-483
1985
Rattus norvegicus
Berge, R.K.; Aarsland, A.
Correlation between the cellular level of long-chain acyl-CoA, peroxisomal beta-oxidation, and palmitoyl-CoA hydrolase activity in rat liver. Are the two enzyme systems regulated by a substrate-induced mechanism?
Biochim. Biophys. Acta
837
141-151
1985
Rattus norvegicus
Berge, R.K.; Nilsson, A.; Husoy, A.M.
Rapid stimulation of liver palmitoyl-CoA synthetase, carnitine palmitoyltransferase and glycerophosphate acyltransferase compared to peroxisomal beta-oxidation and palmitoyl-CoA hydrolase in rats fed high-fat diets
Biochim. Biophys. Acta
960
417-426
1988
Rattus norvegicus
Alexson, S.E.H.; Mentlein, R.; Wernstedt, C.; Hellman, U.
Isolation and characterization of microsomal acyl-CoA thioesterase. A member of the rat liver microsomal carboxylesterase multi-gene family
Eur. J. Biochem.
214
719-727
1993
Rattus norvegicus, Rattus norvegicus (P80250)
Poupon, V.; Begue, B.; Gagnon, J.; Dautry-Varsat, A.; Cerf-Bensussan, N.; Benmerah, A.
Molecular cloning and characterization of MT-ACT48, a novel mitochondrial acyl-CoA thioesterase
J. Biol. Chem.
274
19188-19194
1999
Arabidopsis thaliana, Bacillus subtilis, Caenorhabditis elegans, Drosophila melanogaster, Escherichia coli, Haemophilus influenzae, Helicobacter pylori, Homo sapiens, Mus musculus (Q9R0X4), Oryctolagus cuniculus, Rattus norvegicus
Broustas, C.G.; Larkins, L.K.; Uhler, M.D.; Hajra, A.K.
Molecular cloning and expression of cDNA encoding rat brain cytosolic acyl-coenzyme A thioester hydrolase
J. Biol. Chem.
271
10470-10476
1996
Homo sapiens, Rattus norvegicus
Svensson, L.T.; Alexson, S.E.H.; Hiltunen, J.K.
Very long chain and long chain acyl-CoA thioesterase in rat liver mitochondria
J. Biol. Chem.
270
12177-12183
1995
Rattus norvegicus
Svensson, L.T.; Engberg, S.T.; Aoyama, T.; Usuda, N.; Alexson, S.E.H.; Hashimoto, T.
Molecular cloning and characterization of mitochondrial peroxisome proliferator-induced acyl-CoA thioesterase from rat liver
Biochem. J.
329
601-608
1998
Rattus norvegicus, Rattus norvegicus (O55171), Rattus norvegicus (O88267), Rattus norvegicus (Q64559)
-
Yamada, J.; Matsumoto, I.; Furihata, T.; Sakuma, M.; Suga, T.
Purification and properties of long-chain acyl-CoA hydrolases from the liver cytosol of rats treated with peroxisome proliferator
Arch. Biochem. Biophys.
308
118-125
1994
Rattus norvegicus
Broustas, C.G.; Hajra, A.K.
Purification, properties, and specificity of rat brain cytosolic fatty acyl coenzyme A hydrolase
J. Neurochem.
64
2345-2353
1995
Rattus norvegicus
Yamada, J.; Furihata, T.; Tamura, H.; Watanabe, T.; Suga, T.
Long-chain acyl-CoA hydrolase from rat brain cytosol: purification, characterization, and immunohistochemical localization
Arch. Biochem. Biophys.
326
106-114
1996
Bos taurus, Canis lupus familiaris, Cavia porcellus, Homo sapiens, Mesocricetus auratus, Oryctolagus cuniculus, Platyrrhini, Rattus norvegicus, Sus scrofa
Shin, S.O.; Kameyama, Y.; Yoshida, M.; Takatsu, F.; Shinkai, A.; Inokuchi, H.; Saito, Y.; Yokota, Y.
Characterization of microsomal long-chain acyl-CoA hydrolase activity in the rat submandibular gland
Int. J. Biochem.
26
279-285
1994
Rattus norvegicus
Skorve, J.; Rosendal, J.; Vaagenes, H.; Knudsen, J.; Lillehaug, J.R.; Berge, R.K.
Fatty acyl-CoA oxidase activity is induced before long-chain acyl-CoA hydrolase activity and acyl-CoA binding protein in liver of rat treated with peroxisome proliferating 3-thia fatty acids
Xenobiotica
25
1181-1194
1995
Rattus norvegicus
Sanchez, R.M.; Alegret, M.; Adzet, T.; Merlos, M.; Laguna, J.C.
Differential inhibition of long chain acyl-CoA hydrolases by hypolipidemic drugs in vitro
Biochem. Pharmacol.
43
639-644
1992
Rattus norvegicus
Yamada, J.; Suga, K.; Furihata, T.; Kitahara, M.; Watanabe, T.; Hosokawa, M.; Satoh, T.; Suga, T.
cDNA cloning and genomic organization of peroxisome proliferator-inducible long-chain acyl-CoA hydrolase from rat liver cytosol
Biochem. Biophys. Res. Commun.
248
608-612
1998
Rattus norvegicus
Dixon, A.; Osterloh, J.; Becker, C.
Inhibition of palmitoyl Co-enzyme A hydrolase in mitochondria and microsomes by pharmaceutical organic anions
J. Pharm. Sci.
79
103-105
1990
Rattus norvegicus
Engberg, S.T.; Aoyama, T.; Alexson, S.E.H.; Hashimoto, T.; Svensson, L.T.
Peroxisome proliferator-induced acyl-CoA thioesterase from rat liver cytosol: molecular cloning and functional expression in chinese hamster ovary cells
Biochem. J.
323
525-531
1997
Cricetulus griseus, Rattus norvegicus, Rattus norvegicus (Q64559)
Neuman, I.; Maloberti, P.; Lisdero, C.; Colonna, C.; Peralta, J.; Jose Poderoso, J.; Podesta, E.J.
b-Adrenergic stimulation controls the expression of a thioesterase specific for very-long-chain fatty acids in perfused hearts
Biochem. Biophys. Res. Commun.
299
135-141
2002
Rattus norvegicus
Svensson, L.T.; Wilcke, M.; Alexson, S.E.E.
Peroxisome proliferators differentially regulate long-chain acyl-CoA thioesterases in rat liver
Eur. J. Biochem.
230
813-820
1995
Rattus norvegicus
Garras, A.; Elholm, M.; Sleboda, J.; Froyland, L.; Osmundsen, H.; Berge, R.K.
On the effects of thia fatty acid analogs on hydrolases involved in the degradation of metabolizable and non-metabolizable acyl-CoA esters
Xenobiotica
27
781-799
1997
Rattus norvegicus
Ofman, R.; el Mrabet, L.; Dacremont, G.; Spijer, D.; Wanders, R.J.A.
Demonstration of dimethylnonanoyl-CoA thioesterase activity in rat liver peroxisomes followed by purification and molecular cloning of the thioesterase involved
Biochem. Biophys. Res. Commun.
290
629-634
2002
Rattus norvegicus (Q8VHK0)
Durgan, D.J.; Smith, J.K.; Hotze, M.A.; Egbejimi, O.; Cuthbert, K.D.; Zaha, V.G.; Dyck, J.R.; Abel, E.D.; Young, M.E.
Distinct transcriptional regulation of long-chain acyl-CoA synthetase isoforms and cytosolic thioesterase 1 in the rodent heart by fatty acids and insulin
Am. J. Physiol. Heart Circ. Physiol.
290
H2480-H2497
2006
Rattus norvegicus
Momose, A.; Fujita, M.; Ohtomo, T.; Umemoto, N.; Tanonaka, K.; Toyoda, H.; Morikawa, M.; Yamada, J.
Regulated expression of acyl-CoA thioesterases in the differentiation of cultured rat brown adipocytes
Biochem. Biophys. Res. Commun.
404
74-78
2011
Rattus norvegicus (O55171), Rattus norvegicus (O88267)
Novgorodov, S.A.; Wu, B.X.; Gudz, T.I.; Bielawski, J.; Ovchinnikova, T.V.; Hannun, Y.A.; Obeid, L.M.
Novel pathway of ceramide production in mitochondria: thioesterase and neutral ceramidase produce ceramide from sphingosine and acyl-CoA
J. Biol. Chem.
286
25352-25362
2011
Rattus norvegicus
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