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Information on EC 3.1.2.20 - acyl-CoA hydrolase and Organism(s) Mus musculus and UniProt Accession Q8VHQ9
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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: Mus musculus
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
-
-
-
-
Acot7
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
-
-
-
-
brain acyl-CoA hydrolase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
3-hydroxy-3-methyl glutaryl-CoA + H2O
CoA + 3-hydroxy-3-methyl glutarate
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + H2O
CoA + 3-hydroxy-3-methylglutarate
-
-
-
-
?
DL-3-hydroxy-3-methylglutaryl-CoA + H2O
CoA + 3-hydroxy-3-methylglutarate
-
-
-
-
?
acyl-CoA + H2O
CoA + a carboxylate
-
involved in fatty acid metabolism
-
?
chenodeoxycholoyl-CoA + H2O
CoA + chenodeoxycholoate
activity is PPARalpha-inducible
-
-
?
chenodeoxycholoyl-CoA + H2O
CoA + chenodeoxycholoate
bile acid derivative substrate
-
-
?
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
acyl-CoA + H2O
CoA + a carboxylate
-
involved in fatty acid metabolism
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
optimal range for ionic strength is 80-160 mM for both NaCl and KCl
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acyl-CoA
substrate inhibition at concentrations higher than 0.005-0.01 mM of acyl-CoA longer than C10, BSA protects
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Clofibrate
-
isozymes CTE-I and MTE-I are induced, induction is completely dependent on PPARalpha
PPARalpha
-
internal receptor protein essential for effect of stimulating compounds
-
PPARalpha
internal receptor protein essential for effect of stimulating compounds
-
PPARalpha
-
gene expression inducing and regulatory role, mediates the stimulation by clofibrate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0106
myristoyl-CoA
-
at 37°C, in the presence of StarD2 protein in a molar ratio StarD2/Them2 of 0.5
0.0136
myristoyl-CoA
-
at 37°C, in the presence of StarD2 protein in a molar ratio StarD2/Them2 of 1.0
0.0228
myristoyl-CoA
-
at 37°C, in the presence of small unilamellar vesicles composed of phosphatidylcholine at 4 mM total phospholipid concentration
0.0159
palmitoyl-CoA
-
in the presence of StarD2 protein in a molar ratio StarD2/Them2 of 1.0
0.018
palmitoyl-CoA
-
in the presence of StarD2 protein in a molar ratio StarD2/Them2 of 0.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
inactive with acetyl-CoA and 2-butenoyl-CoA
-
0.033
myristoyl-CoA
-
at 37°C, in the presence of small unilamellar vesicles composed of phosphatidylcholine at 4 mM total phospholipid concentration
0.069
myristoyl-CoA
-
at 37°C, in the presence of StarD2 protein in a molar ratio StarD2/Them2 of 0.5
0.086
myristoyl-CoA
-
at 37°C, in the presence of StarD2 protein in a molar ratio StarD2/Them2 of 1.0
0.0066
palmitoyl-CoA
-
in the presence of StarD2 protein in a molar ratio StarD2/Them2 of 1.0
0.057
palmitoyl-CoA
-
in the presence of StarD2 protein in a molar ratio StarD2/Them2 of 0.5
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.4
myristoyl-CoA
-
at 37°C, in the presence of small unilamellar vesicles composed of phosphatidylcholine at 4 mM total phospholipid concentration
6
myristoyl-CoA
-
at 37°C, in the presence of StarD2 protein in a molar ratio StarD2/Them2 of 0.5
6
myristoyl-CoA
-
at 37°C, in the presence of StarD2 protein in a molar ratio StarD2/Them2 of 1.0
3
palmitoyl-CoA
-
in the presence of StarD2 protein in a molar ratio StarD2/Them2 of 0.5
4
palmitoyl-CoA
-
in the presence of StarD2 protein in a molar ratio StarD2/Them2 of 1.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0322
-
substrate myristoyl-CoA, at 37°C, in the presence of small unilamellar vesicles composed of phosphatidylcholine at 4 mM total phospholipid concentration
0.0568
-
substrate palmitoyl-CoA, in the presence of StarD2 protein in a molar ratio StarD2/Them2 of 0.5
0.0652
-
substrate palmitoyl-CoA, in the presence of StarD2 protein in a molar ratio StarD2/Them2 of 1.0
0.0681
-
substrate myristoyl-CoA, at 37°C, in the presence of StarD2 protein in a molar ratio StarD2/Them2 of 0.5
0.0846
-
substrate myristoyl-CoA, at 37°C, in the presence of StarD2 protein in a molar ratio StarD2/Them2 of 1.0
additional information
-
in mesenteric lymph nodes of mice fasted for 16 h, ACOT7 levels are induced 1.8fold, which reflect a 1.5fold increase in enzyme activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
before postnatal day 10, brain acyl-CoA hydrolase is detected at very low levels. Then, brain acyl-CoA hydrolase content rapidly increases from P14 and reaches maximum levels at P21, remaining high until at least P70. The increase in brain acyl-CoA hydrolase content corresponds to the appearance of pachytene spermatocytes
additional information
-
brain acyl-CoA hydrolase is not detected in spermatogonia and mature spermatozoa
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
doubling cytosolic enzyme activity fails to protect mice from diet-induced obesity, fatty liver or insulin resistance, however, overexpression of isoform Acot7 in adipocytes renders mice cold intolerant
malfunction
-
ACOT7 knockout mice in the nervous system, reveal increased fatty acid flux into multiple long-chain acyl-CoA-dependent pathways. The alterations in brain fatty acid metabolism are concomitant with a loss of lean mass, hypermetabolism, hepatic steatosis, dyslipidemia, and behavioral hyperexcitability in Acot7 N-/- mice
malfunction
-
Ad-Acot2 mice have higher free fatty acid utilization during the rest phase of the day but readily switch to carbohydrate oxidation at night. In isolated Ad-Acot2 liver mitochondria, phosphorylating O2 consumption is elevated with lipid but not non-lipid substrate. While the monolysocardiolipin pool in expanded in Ad-Acot2 liver mitochondria, total cardiolipin is unchanged
malfunction
-
Them5 knockout mice display changes in the lipid profile of cardiolipin and its metabolites. Them5 loss results in an 2fold decrease in free fatty acids in mitochondria, with a particularly marked decrease in linoleic and linolenic acids in the knockout samples. Them5 knockout mice develop fatty liver. In addition, loss of thioesterase activity of Them5 leads to changes in mitochondrial morphology and function
malfunction
-
Them5-/- mice show deregulation of lipid metabolism and the development of fatty liver, exacerbated by a high-fat diet. Mitochondrial morphology is affected, and functions such as respiration and beta-oxidation are impaired
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no glycoprotein
p48 is not N-glycosylated and does not enter the secretion pathway
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
thioesterase domain alone of Them1 is sufficient to yield active recombinant protein, START domain is required for optimal enzyme activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
Tm 59.2°C (transition beginning at temperatures in excess of 50°C)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, expression in Escherichia coli BL21(DE3)
from murine EST library, DNA and amino acid sequence determination and analysis, transient expression in HeLa cells, expression as inactive GST-fusion protein in bacteria
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform Acot11 is up-regulated in adipose and liver during conditions that increase lipid anabolic processes, specifically Acot11 is up-regulated 10 and 34fold in FR (control diet fed mice fasted for 14 hours then refed for 12 hours overnight) gonadal white adipose tissue and inguinal white adipose tissue, respectively, and 5fold and 13fold in liver during FR and high-fat diet, respectively
in mesenteric lymph nodes of mice fasted for 16 h, ACOT7 levels are induced 1.8fold, which reflect a 1.5fold increase in enzyme activity
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Hunt, M.C.; Lindquist, P.J.G.; Peters, J.M.; Gonzalez, F.J.; Diczfalusy, U.; Alexson, S.E.H.
Involvement of the peroxisome proliferator-activated receptor a in regulating long-chain acyl-CoA thioesterases
J. Lipid Res.
41
814-823
2000
Mus musculus
Hunt, M.C.; Solaas, K.; Kase, B.F.; Alexson, S.E.
Characterization of an acyl-coA thioesterase that functions as a major regulator of peroxisomal lipid metabolism
J. Biol. Chem.
277
1128-1138
2002
Mus musculus (P58137)
Hunt, M.; Lindquist, P.J.G.; Nousiainen, S.; Svensson, T.L.T.; Diczfalusy, U.; Alexson, S.E.H.
Cloning and regulation of peroxisome proliferator-induced acyl-CoA thioesterases from mouse liver
Adv. Exp. Med. Biol.
466
195-200
1999
Mus musculus
Takagi, M.; Ohtomo, T.; Hiratsuka, K.; Kuramochi, Y.; Suga, T.; Yamada, J.
Localization of a long-chain acyl-CoA hydrolase in spermatogenic cells in mice
Arch. Biochem. Biophys.
446
161-166
2006
Mus musculus
Golovko, M.Y.; Rosenberger, T.A.; Faergeman, N.J.; Feddersen, S.; Cole, N.B.; Pribill, I.; Berger, J.; Nussbaum, R.L.; Murphy, E.J.
Acyl-CoA synthetase activity links wild-type but not mutant alpha-synuclein to brain arachidonate metabolism
Biochemistry
45
6956-6966
2006
Mus musculus
Westin, M.A.; Hunt, M.C.; Alexson, S.E.
Short- and medium-chain carnitine acyltransferases and acyl-CoA thioesterases in mouse provide complementary systems for transport of beta-oxidation products out of peroxisomes
Cell. Mol. Life Sci.
65
982-990
2008
Mus musculus
Wei, J.; Kang, H.W.; Cohen, D.E.
Thioesterase superfamily member 2 (Them2)/acyl-CoA thioesterase 13 (Acot13): a homotetrameric hotdog fold thioesterase with selectivity for long-chain fatty acyl-CoAs
Biochem. J.
421
311-322
2009
Mus musculus
Ohtomo, T.; Nakao, C.; Sumiya, M.; Kaminuma, O.; Abe, A.; Mori, A.; Inaba, N.; Kato, T.; Yamada, J.
Identification of acyl-CoA thioesterase in mouse mesenteric lymph nodes
Biol. Pharm. Bull.
36
866-871
2013
Mus musculus
Han, S.; Cohen, D.E.
Functional characterization of thioesterase superfamily member 1/Acyl-CoA thioesterase 11: implications for metabolic regulation
J. Lipid Res.
53
2620-2631
2012
Mus musculus
Moffat, C.; Bhatia, L.; Nguyen, T.; Lynch, P.; Wang, M.; Wang, D.; Ilkayeva, O.R.; Han, X.; Hirschey, M.D.; Claypool, S.M.; Seifert, E.L.
Acyl-CoA thioesterase-2 facilitates mitochondrial fatty acid oxidation in the liver
J. Lipid Res.
55; 2458-2470
2458-2470
2014
Mus musculus
Zhuravleva, E.; Gut, H.; Hynx, D.; Marcellin, D.; Bleck, C.K.; Genoud, C.; Cron, P.; Keusch, J.J.; Dummler, B.; Esposti, M.D.; Hemmings, B.A.
Acyl coenzyme A thioesterase Them5/Acot15 is involved in cardiolipin remodeling and fatty liver development
Mol. Cell. Biol.
32
2685-2697
2012
Mus musculus, Homo sapiens (Q5T1C6)
Ellis, J.M.; Wong, G.W.; Wolfgang, M.J.
Acyl coenzyme A thioesterase 7 regulates neuronal fatty acid metabolism to prevent neurotoxicity
Mol. Cell. Biol.
33
1869-1882
2013
Mus musculus
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