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Information on EC 2.3.1.16 - acetyl-CoA C-acyltransferase and Organism(s) Rattus norvegicus and UniProt Accession Q64428
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2.3.1.16 acetyl-CoA C-acyltransferaseIUBMB Comments
The enzyme, found in both eukaryotes and in prokaryotes, is involved in degradation pathways such as fatty acid beta-oxidation. The enzyme acts on 3-oxoacyl-CoAs to produce acetyl-CoA and an acyl-CoA shortened by two carbon atoms. The reaction starts with the acylation of a nucleophilic cysteine at the active site by a 3-oxoacyl-CoA, with the concomitant release of acetyl-CoA. In the second step the acyl group is transferred to CoA. Most enzymes have a broad substrate range for the 3-oxoacyl-CoA. cf. EC 2.3.1.9, acetyl-CoA C-acetyltransferase.
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Word Map
- 2.3.1.16
- peroxisomal
-
beta-oxidation
-
polyunsaturated
-
pufas
-
hydratase
- enoyl-coa
- 3-hydroxyacyl-coa
-
elovls
-
docosahexaenoic
- polyhydroxyalkanoate
-
monounsaturated
-
lc-pufas
- carnitine
-
desaturases
-
lipogenesis
-
trifunctional
-
desaturation
-
lipogenic
-
eicosapentaenoic
- eutropha
-
ralstonia
- stearoyl-coa
-
thiolytic
- acylcarnitine
- zellweger
- trimetazidine
-
hadhb
-
siganus
- punctata
-
chondrodysplasia
-
poly3-hydroxybutyrate
- srebp-1
-
rhizomelic
- glyoxysomal
-
phytanic
-
acetoacetyl-coenzyme
- 3-hydroxybutyrate
- adrenoleukodystrophy
- plasmalogens
-
antianginal
-
very-long-chain
- poly-beta-hydroxybutyrate
-
linseed
-
ketoacidotic
-
palmitoleic
- acaca
- medicine
- agriculture
- synthesis
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
elovl6, elovl5, 3-ketoacyl-coa thiolase, beta-ketothiolase, 3-oxoacyl-coa thiolase, acaa2, 3-ketothiolase, elovl-6, thiolase i, thiolase a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein
-
3-ketoacyl CoA thiolase
-
-
-
-
3-ketoacyl coenzyme A thiolase
-
-
-
-
3-ketoacyl thiolase
-
-
-
-
3-ketoacyl-CoA thiolase
3-ketothiolase
-
-
-
-
3-oxoacyl-CoA thiolase
-
-
-
-
3-oxoacyl-coenzyme A thiolase
-
-
-
-
6-oxoacyl-CoA thiolase
-
-
-
-
acetoacetyl-CoA beta-ketothiolase
-
-
-
-
acetyl-CoA acyltransferase
-
-
-
-
acyltransferase, acetyl coenzyme A
-
-
-
-
beta-ketoacyl coenzyme A thiolase
-
-
-
-
beta-ketoacyl-CoA thiolase
-
-
-
-
beta-ketoadipyl coenzyme A thiolase
-
-
-
-
beta-ketoadipyl-CoA thiolase
-
-
-
-
beta-ketothiolase
-
-
-
-
KAT
-
-
-
-
ketoacyl-CoA acyltransferase
-
-
-
-
ketoacyl-coenzyme A thiolase
-
-
-
-
long-chain 3-oxoacyl-CoA thiolase
-
-
-
-
oxoacyl-coenzyme A thiolase
-
-
-
-
pro-3-ketoacyl-CoA thiolase
-
-
-
-
SCP2/3-oxoacyl-CoA thiolase
-
-
-
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thiloase B
-
-
-
-
thiolase A
-
-
-
-
thiolase I
-
-
-
-
thiolase II
-
-
-
-
thiolase III
-
-
-
-
3-ketoacyl-CoA thiolase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
multifunctional enzyme: 2-enoyl-CoA hydratase, 3-ketoacyl-CoA thiolase, 3-hydroxyacyl-CoA dehydrogenase
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
sterol carrier protein X is a 3-oxoacyl CoA thiolase with intrinsic sterol carrier and lipid transfer activity
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
alpha-Linolenic acid metabolism, Benzoate degradation, Biosynthesis of secondary metabolites, Biosynthesis of unsaturated fatty acids, Ethylbenzene degradation, Fatty acid degradation, Fatty acid elongation, Geraniol degradation, Microbial metabolism in diverse environments, Valine, leucine and isoleucine degradation
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:acetyl-CoA C-acyltransferase
The enzyme, found in both eukaryotes and in prokaryotes, is involved in degradation pathways such as fatty acid beta-oxidation. The enzyme acts on 3-oxoacyl-CoAs to produce acetyl-CoA and an acyl-CoA shortened by two carbon atoms. The reaction starts with the acylation of a nucleophilic cysteine at the active site by a 3-oxoacyl-CoA, with the concomitant release of acetyl-CoA. In the second step the acyl group is transferred to CoA. Most enzymes have a broad substrate range for the 3-oxoacyl-CoA. cf. EC 2.3.1.9, acetyl-CoA C-acetyltransferase.
CAS REGISTRY NUMBER
COMMENTARY
9029-97-4
-
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
dodecanoyl-CoA + H2O
dodecanoate + CoA
-
acetyl-CoA hydrolase activity
-
-
?
acetyl-CoA + H2O
acetate + CoA
-
best acyl-CoA substrate, acetyl-CoA hydrolase activity
-
-
?
acetyl-CoA + H2O
acetate + CoA
-
preferred substrate, 3-ketoacyl-CoA thiolase activity
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
enzyme catalyses the last step in the beta-oxidation cycle
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
enzyme plays important role in peroxisomal beta-oxidation, in addition the enzyme may facilitate the intraperoxysomal movement of sterols and certain other lipids
-
-
?
CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
-
highest activity with 3-oxohexanoyl-CoA
-
-
r
additional information
?
-
-
3-oxoacyl-CoA homologues from acetoacetyl to 3-oxopalmitoyl-CoA
-
-
?
additional information
?
-
-
thiolase A and B possess virtually the same substrate specificity
-
-
?
additional information
?
-
-
key enzyme involved in fatty acid oxidation
-
-
?
additional information
?
-
-
the enzyme is involved in fatty acid beta-oxidation
-
-
?
additional information
?
-
-
analysis of the substrate chain length specificity of the enzyme, high preference for acetyl-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
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
enzyme catalyses the last step in the beta-oxidation cycle
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
enzyme plays important role in peroxisomal beta-oxidation, in addition the enzyme may facilitate the intraperoxysomal movement of sterols and certain other lipids
-
-
?
additional information
?
-
-
key enzyme involved in fatty acid oxidation
-
-
?
additional information
?
-
-
the enzyme is involved in fatty acid beta-oxidation
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetoacetyl-CoA
-
competitive inhibition of the acetyl-CoA hydrolase activity
acetyl-CoA
-
competitive inhibition of the 3-ketoacyl-CoA thiolase activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
overview: Km of peroxisomal and mitochondrial enzyme with various substrates
-
additional information
additional information
-
overview: Km of peroxisomal and mitochondrial enzyme with various substrates
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.24
acetyl-CoA
-
pH 7.4, competitive versus 3-ketoacyl-CoA thiolase activity
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
di-(2-ethylhexyl)phthalate-inducible acetyl-CoA hydrolase activity
-
di-(2-ethylhexyl)phthalate-inducible acetyl-CoA hydrolase activity
-
di-(2-ethylhexyl)phthalate-inducible acetyl-CoA hydrolase activity
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme is synthesized in the cytosol and subsequently imported into the peroxisome
-
thiolase A from normal rat liver peroxisomes and thiolase B from livers of clofibrate-treated rats
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
Elovl-5 knockdown decreases elongation of 16:1,n-7. Elovl-5 over-expression increases synthesis of 18:1,n-7, however, this is dependent on stearoyl-CoA desaturase driven 16:1,n-7 availability
physiological function
-
knockdown of Elovl-6 decreases elongation of 16:0 and 16:1,n-7, resulting in accumulation of 16:1,n-7. Elovl-6 over-expression preferentially drives synthesis of 16:0 elongation products 18:0 and 18:1,n-9 but not 18:1,n-7
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
460000
41000
460000
multifunctional enzyme: 2-enoyl-CoA hydratase, 3-ketoacyl-CoA thiolase, 3-hydroxyacyl-CoA dehydrogenase, gel filtration
41000
-
2 * 41000, SDS-PAGE, thiolase B dimer dissociates into monomer with low activity during cold inactivation, thiolase A maintains its dimeric structure
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
-
2 * 41000, SDS-PAGE, thiolase B dimer dissociates into monomer with low activity during cold inactivation, thiolase A maintains its dimeric structure
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H352A
-
3.3fold increase in KM-value for acetoacetyl-CoA compared to wild-type value, Vmax is decreased 1154 times
H352E
-
2.7fold increase in KM-value for acetoacetyl-CoA compared to wild-type value, Vmax is decreased 1250 times
H352K
-
3.7fold increase in KM-value for acetoacetyl-CoA compared to wild-type value, Vmax is decreased 526 times
H352Y
-
3.1fold increase in KM-value for acetoacetyl-CoA compared to wild-type value, Vmax is decreased 429 times
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
thiolase B exhibits cold-lability: loss of acitvity is more pronounced at 4°C than at 30°C, in the presence of KCl, thiolase A is stable under the same conditions, thiolase A exhibits higher stabiliy than thiolase B at 46°C, lability of the thiolase B might be compensated for by the formation of a more stable multienzyme complex
additional information
-
enzyme exhibits reversible cold-lability: loss of acitvity at 4°C in the presence of NaCl, half-maximal inactivation in ice in 4 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, wild-type and mutant enzymes H352E, H352A, H352K and H352Y, stable for at least 3 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 27.2fold from liver mitochondria preparation by 5 steps of ion exchange and hydrophobic interaction chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged wild-type and His352 mutant proteins overexpressed in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Seedorf, U.; Brysch, P.; Engel, T.; Schrage, K.; Assmann, G.
Sterol carrier protein x is peroxisomal 3-oxoacyl coenzyme A thiolase with intrinsic sterol carrier and lipid transfer activity
J. Biol. Chem.
269
21277-21283
1994
Rattus norvegicus
Miyazawa, S.; Osumi, T.; Hashimoto, T.
The presence of a new 3-oxoacyl-CoA thiolase in rat liver peroxisomes
Eur. J. Biochem.
103
589-596
1980
Rattus norvegicus
Miyazawa, S.; Furuta, S.; Osumi, T.; Hashimoto, T.; Ui, N.
Properties of peroxisomal 3-ketoacyl-CoA thiolase from rat liver
J. Biochem.
90
511-519
1981
Rattus norvegicus
Uchida, Y.; Izai, K.; Orii, T.; Hashimoto, T.
Novel fatty acid beta-oxidation enzymes in rat liver mitochondria. II. Purification and properties of enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein
J. Biol. Chem.
267
1034-1041
1992
Rattus norvegicus, Rattus norvegicus (Q64428)
Middleton, B.
3-Ketoacyl-CoA thiolase of mammalian tissues
Methods Enzymol.
35 B
128-136
1975
Bos taurus, Ovis aries, Rattus norvegicus, Sus scrofa
-
Li, J.; Schulz, H.
4-Bromo-2-octenoic acid specifically inactivates 3-ketoacyl-CoA thiolase and thereby fatty acid oxidation in rat liver mitochondria
Biochemistry
27
5995-6000
1988
Rattus norvegicus
Arakawa, H.; Takiguchi, M.; Amaya, Y.; Nagata, S.; Hayashi, H.; Mori, M.
cDNA-derived amino acid sequence of rat mitochondrial 3-oxoacyl-CoA thiolase with no transient presequence: structural relationship with peroxisomal isozyme
EMBO J.
6
1361-1366
1987
Rattus norvegicus
Krahling, J.B.; Tolbert, N.E.
Peroxisomal beta-ketothiolase
Arch. Biochem. Biophys.
209
100-110
1981
Rattus norvegicus
Antonenkov, V.D.; Van Veldhoven, P.P.; Waelkens, E.; Mannaerts, G.P.
Comparison of the stability and substrate specificity of purified peroxisomal 3-oxoacyl-CoA thiolases A and B from rat liver
Biochim. Biophys. Acta
1437
136-141
1999
Rattus norvegicus
Latruffe, N.; Nicolas-Frances, V.; Dasari, V.K.; Osumi, T.
Studies on regulation of the peroxisomal beta-oxidation at the 3-ketothiolase step: Dissection of the rat liver thiolase B gene promoter
Adv. Exp. Med. Biol.
466
253-259
1999
Rattus norvegicus
Zeng, J.; Li, D.
Expression and purification of His-tagged rat mitochondrial 3-ketoacyl-CoA thiolase wild-type and His352 mutant proteins
Protein Expr. Purif.
35
320-326
2004
Rattus norvegicus
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
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