Information on EC 2.3.1.16 - acetyl-CoA C-acyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
2.3.1.16
-
RECOMMENDED NAME
GeneOntology No.
acetyl-CoA C-acyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
show the reaction diagram
multienzyme complex: 3-hydroxyacyl-coenzyme A epimerase, cis-DELTA3-trans-DELTA2-enoyl-CoA isomerase, enoyl-CoA hydratase, L-3-hydroxyacyl-CoA thiolase
-
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
show the reaction diagram
multienzyme complex: EC 4.2.1.17, EC 1.1.1.35, EC 5.3.3.3, EC 5.1.2.3, EC 2.3.1.16
-
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
show the reaction diagram
multienzyme complex: EC 4.2.1.17, EC 1.1.1.35, EC 5.3.3.3, EC 5.1.2.3, EC 2.3.1.16
-
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
show the reaction diagram
ping-pong mechanism; sterol carrier protein X is a 3-oxoacyl CoA thiolase with intrinsic sterol carrier and lipid transfer activity
-
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
show the reaction diagram
ping-pong mechanism
-
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
show the reaction diagram
multifunctional enzyme: 2-enoyl-CoA hydratase, 3-ketoacyl-CoA thiolase, 3-hydroxyacyl-CoA dehydrogenase
Q64428
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
show the reaction diagram
multienzyme complex contains enoyl-CoA hydratase, L-3-hydroxyacyl-CoA dehydrogenase, 3-ketoacyl-CoA thiolase, 3-hydroxyacyl-CoA epimerase : EC 5.1.2.3 and DELTA3-cis-DELTA-trans-enoyl-CoA isomerase: EC 5.3.3.3
-
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
show the reaction diagram
multifunctional enzyme: 2-enoyl-CoA hydratase, 3-ketoacyl-CoA thiolase and long-chain specific 3-hydroxyacyl-CoA dehydrogenase
-
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
show the reaction diagram
multifunctional enzyme: 2-enoyl-CoA hydratase, 3-ketoacyl-CoA thiolase, 3-hydroxyacyl-CoA dehydrogenase
P28790
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
show the reaction diagram
Claisen condensation
-
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
show the reaction diagram
stoichiometry
-
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
show the reaction diagram
reaction mechanism
P27796
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
show the reaction diagram
the active site involves residues Cys138, in loop beta4alpha3 on domain I, His393 on the segment linking alpha10 and alpha11 of domain III, and Cys425 at the C-terminal end of beta12, detailed reaction mechanism, overview
Q56WD9
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
show the reaction diagram
ping-pong mechanism, a cysteine residue in involved in the active site
-
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
show the reaction diagram
multienzyme complex: EC 4.2.1.17, EC 1.1.1.35, EC 5.3.3.3, EC 5.1.2.3, EC 2.3.1.16
Escherichia coli B.
-
-
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
show the reaction diagram
multifunctional enzyme: 2-enoyl-CoA hydratase, 3-ketoacyl-CoA thiolase, 3-hydroxyacyl-CoA dehydrogenase
Pseudomonas fragi B-0771, Rattus norvegicus Wistar
-
-
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
Acyl group transfer
-
-
Claisen condensation
-
-
PATHWAY
KEGG Link
MetaCyc Link
10-cis-heptadecenoyl-CoA degradation (yeast)
-
10-trans-heptadecenoyl-CoA degradation (MFE-dependent, yeast)
-
10-trans-heptadecenoyl-CoA degradation (reductase-dependent, yeast)
-
4-hydroxybenzoate biosynthesis V
-
9-cis, 11-trans-octadecadienoyl-CoA degradation (isomerase-dependent, yeast)
-
alpha-Linolenic acid metabolism
-
Benzoate degradation
-
Biosynthesis of secondary metabolites
-
Biosynthesis of unsaturated fatty acids
-
cholesterol degradation to androstenedione I (cholesterol oxidase)
-
cholesterol degradation to androstenedione II (cholesterol dehydrogenase)
-
Ethylbenzene degradation
-
fatty acid beta-oxidation (peroxisome, yeast)
-
fatty acid beta-oxidation I
-
fatty acid beta-oxidation II (peroxisome)
-
fatty acid beta-oxidation VI (peroxisome)
-
Fatty acid degradation
-
Fatty acid elongation
-
fatty acid salvage
-
Geraniol degradation
-
jasmonic acid biosynthesis
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
pyruvate fermentation to hexanol
-
sitosterol degradation to androstenedione
-
Valine, leucine and isoleucine degradation
-
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:acetyl-CoA C-acyltransferase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase/3-oxoacyl-CoA thiolase
-
-
3-KAT
-
-
3-ketoacyl CoA thiolase
-
-
-
-
3-ketoacyl coenzyme A thiolase
-
-
-
-
3-ketoacyl coenzyme-A thiolase
-
-
3-ketoacyl thiolase
-
-
-
-
3-ketoacyl-CoA thiolase
-
-
-
-
3-ketoacyl-CoA thiolase
Q56WD9
-
3-ketoacyl-CoA thiolase
-
-
3-ketoacyl-CoA thiolase
Q6TXD0
-
3-ketoacyl-CoA thiolase
-
-
3-ketoacyl-CoA thiolase
Q8VCH0, Q921H8
-
3-ketoacyl-CoA thiolase
-
-
3-ketothiolase
-
-
-
-
3-oxoacyl-CoA thiolase
-
-
-
-
3-oxoacyl-coenzyme A thiolase
-
-
-
-
3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase
-
-
6-oxoacyl-CoA thiolase
-
-
-
-
acetoacetyl-CoA beta-ketothiolase
-
-
-
-
acetyl-CoA acyltransferase
-
-
-
-
acyl-CoA-thiolase
-
-
acyltransferase, acetyl coenzyme A
-
-
-
-
beta-ketoacyl coenzyme A thiolase
-
-
-
-
beta-ketoacyl-CoA thiolase
-
-
-
-
beta-ketoadipyl coenzyme A thiolase
-
-
-
-
beta-ketoadipyl-CoA thiolase
-
-
-
-
beta-ketothiolase
-
-
-
-
beta-ketothiolase
-
-
beta-ketothiolase
-
-
ELo1
Parietochloris incisa
B8YJJ0
-
ELOVL5
-
-
enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein
Q64428
-
fatty acid elongase 5
-
-
KAT
-
-
-
-
KAT2
Q6W6X6
-
ketoacyl-CoA acyltransferase
-
-
-
-
ketoacyl-coenzyme A thiolase
-
-
-
-
long-chain 3-oxoacyl-CoA thiolase
-
-
-
-
oxoacyl-coenzyme A thiolase
-
-
-
-
pro-3-ketoacyl-CoA thiolase
-
-
-
-
PUFA elongase
Parietochloris incisa
B8YJJ0
-
SCP2/3-oxoacyl-CoA thiolase
-
-
-
-
sterol carrier protein 2/3-oxoacyl-CoA thiolase
Q66Q58
-
thiloase B
-
-
-
-
thiolase A
-
-
-
-
thiolase I
-
-
-
-
thiolase II
-
-
-
-
thiolase III
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9029-97-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
isoform KAT2
SwissProt
Manually annotated by BRENDA team
precursor
SwissProt
Manually annotated by BRENDA team
representative and intermediate strains
-
-
Manually annotated by BRENDA team
Pex5pM mutant
-
-
Manually annotated by BRENDA team
basonym Alcaligenes eutrophus
-
-
Manually annotated by BRENDA team
ML308-225, D-1ML, K-12-Y Mel and fatty degradation mutants: fad-5, fadB64, fadA30
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
isoform Elovl6
-
-
Manually annotated by BRENDA team
isoform Elovl6
UniProt
Manually annotated by BRENDA team
3-ketoacyl-CoA thiolase A
SwissProt
Manually annotated by BRENDA team
3-ketoacyl-CoA thiolase B
SwissProt
Manually annotated by BRENDA team
male
-
-
Manually annotated by BRENDA team
Parietochloris incisa
-
UniProt
Manually annotated by BRENDA team
Pseudomonas fragi B-0771
B-0771
UniProt
Manually annotated by BRENDA team
gene paaJ
-
-
Manually annotated by BRENDA team
gene paaJ
-
-
Manually annotated by BRENDA team
male Wistar rats
-
-
Manually annotated by BRENDA team
strain HB8
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-
the enzyme PaaJ is involved in the aerobic phenylacetate catabolic pathway. PaaJ, a beta-ketothiolase, transforms the resulting beta-keto C8 intermediate with CoA to the C6 intermediate dehydroadipyl-CoA and acetyl-CoA, besides catalyzing the last step of the pathway, in which 3-oxoadipyl-CoA similarly is cleaved to acetyl-CoA and succinyl-CoA
metabolism
-
the enzyme is involved in acyclic terpenes utilisation and leucine/isovalerate utilisation pathways which are connected by the beta-oxidation phase, overview
metabolism
-
the enzyme PaaJ is involved in the aerobic phenylacetate catabolic pathway. PaaJ, a beta-ketothiolase, transforms the resulting beta-keto C8 intermediate with CoA to the C6 intermediate dehydroadipyl-CoA and acetyl-CoA, besides catalyzing the last step of the pathway, in which 3-oxoadipyl-CoA similarly is cleaved to acetyl-CoA and succinyl-CoA
-
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; 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
physiological function
-
in mice deficient for isoform Thb, the degree of induction of peroxisomal beta-oxidation of palmitate mediated by Wy14,643, a synthetic compound activating nuclear hormone receptor PPARalpha, is significantly reduced in mice deficient for Thb, while mitochondrial beta-oxidation is unaltered. The thiolase step alone is responsible for the reduced peroxisomal beta-oxidation of fatty acids. Peroxisome proliferation in the liver after Wy-treatment is normal in Thb -/- mice
physiological function
Q56WD9
isoform KAT2 positively regulates abscisic acid signaling in all the major abscisic acid responses, including abscisic acid-induced inhibition of seed germination and post-germination growth arrest, and abscisic acid-induced stomatal closure and stomatal opening inhibition in Arabidopsis thaliana. KAT2 is shown to be important for reactive oxygen species production in response to abscisic acid. Additionally, KAT2 may function downstream of transcription repressor WRKY40, which may link KAT2 with abscisic acid receptor ABAR/CHLH-mediated signaling
physiological function
Q22100
loss-of-function mutations of the ketoacyl thiolase gene kat-1 result in an increased accumulation of the lipofuscin-like fluorescent aging pigment, shortened lifespan, early behavioral decline, and other abnormalities characteristic of premature aging. Isoform kat-1 is required for the extension of lifespan and enhanced thermotolerance mediated by extra copies of the deacetylase gene sir-2.1. kat-1 acts independently of other known pathways that affect longevity
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,4-dichlorophenoxybutyric acid + acetyl-CoA
?
show the reaction diagram
-
-
-
-
?
3-oxo-5,6-dehydrosuberyl-CoA + CoA
2,3-dehydroadipyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
?
5-methyl-3-oxo-4-hexenoyl-CoA + CoA
3-methylcrotonyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
?
7-methyl-3-oxo-6-octenoyl-CoA + CoA
5-methylhex-4-enoyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
?
acetyl-CoA + H2O
acetate + CoA
show the reaction diagram
-
-
-
-
r
acetyl-CoA + H2O
acetate + CoA
show the reaction diagram
-
3-ketoacyl-CoA thiolase activity, best acyl-CoA substrate, acetyl-CoA hydrolase activity, preferred substrate, 3-ketoacyl-CoA thiolase activity
-
-
?
acyl-CoA + acetyl-CoA
CoA + 3-oxoacyl-CoA
show the reaction diagram
-
-
-
-
?
butyryl-CoA + H2O
butyrate + CoA
show the reaction diagram
-
acetyl-CoA hydrolase activity
-
-
?
CoA + 3-ketolauryl-CoA
acetyl-CoA + decanoyl-CoA
show the reaction diagram
-
-
-
-
?
CoA + 3-ketolauryl-CoA
acetyl-CoA + decanoyl-CoA
show the reaction diagram
-
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
Q64428
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
P28790
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
two-step reaction
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
P27796
two-step reaction
-
r
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
two-step reaction
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
enzyme catalyses the last step in the beta-oxidation cycle
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
enzyme catalyses the last step in the beta-oxidation cycle
-
-
r
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
enzyme catalyses the last step in the beta-oxidation cycle
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
P27796
enzyme catalyses the last step in the beta-oxidation cycle
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
enzyme catalyses the last step in the beta-oxidation cycle
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
Q56WD9
metabolism in the peroxisome influences metabolism in the lipid body
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
enzyme catalyses step of fatty acid beta-oxidation
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
enzyme catalyses step of fatty acid beta-oxidation
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
Q56WD9
enzyme catalyses step of fatty acid beta-oxidation
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
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-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
Escherichia coli B.
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
Pseudomonas fragi B-0771
P28790
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
Rattus norvegicus Wistar
-
-
-
-
CoA + 3-oxodecanoyl-CoA
acetyl-CoA + octanoyl-CoA
show the reaction diagram
-
-
-
-
-
CoA + 3-oxodecanoyl-CoA
acetyl-CoA + octanoyl-CoA
show the reaction diagram
-
-
-
-
?
CoA + 3-oxodecanoyl-CoA
acetyl-CoA + octanoyl-CoA
show the reaction diagram
-
-
-
-
?
CoA + 3-oxodecanoyl-CoA
acetyl-CoA + octanoyl-CoA
show the reaction diagram
-
-
-
-
r
CoA + 3-oxodecanoyl-CoA
acetyl-CoA + octanoyl-CoA
show the reaction diagram
-
-
-
-
-
CoA + 3-oxodecanoyl-CoA
acetyl-CoA + octanoyl-CoA
show the reaction diagram
-
-
-
-
r
CoA + 3-oxododecanoyl-CoA
acetyl-CoA + decanoyl-CoA
show the reaction diagram
-
-
-
-
?
CoA + 3-oxododecanoyl-CoA
acetyl-CoA + decanoyl-CoA
show the reaction diagram
-
-
-
-
?
CoA + 3-oxododecanoyl-CoA
acetyl-CoA + decanoyl-CoA
show the reaction diagram
-
-
-
-
?
CoA + 3-oxoheptanoyl-CoA
acetyl-CoA + pentanoyl-CoA
show the reaction diagram
-
-
-
-
r
CoA + 3-oxohexadecanoyl-CoA
acetyl-CoA + tetradecanoyl-CoA
show the reaction diagram
-
-
-
-
?
CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
show the reaction diagram
-
-
-
-
?
CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
show the reaction diagram
-
-
-
-
?
CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
show the reaction diagram
-
-
-
-
r
CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
show the reaction diagram
-
-
-
-
?
CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
show the reaction diagram
-
-
-
-
?
CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
show the reaction diagram
-
-
-
-
?
CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
show the reaction diagram
-
highest activity with 3-oxohexanoyl-CoA
-
-
r
CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
show the reaction diagram
-
highest activity with 3-oxohexanoyl-CoA
-
-
-
CoA + 3-oxooctanoyl-CoA
acetyl-CoA + hexanoyl-CoA
show the reaction diagram
-
-
-
-
?
CoA + 3-oxooctanoyl-CoA
acetyl-CoA + hexanoyl-CoA
show the reaction diagram
-
-
-
-
?
CoA + 3-oxooctanoyl-CoA
acetyl-CoA + hexanoyl-CoA
show the reaction diagram
-
-
-
-
r
CoA + 3-oxooctanoyl-CoA
acetyl-CoA + hexanoyl-CoA
show the reaction diagram
-
-
-
-
?
CoA + 3-oxooctanoyl-CoA
acetyl-CoA + hexanoyl-CoA
show the reaction diagram
-
-
-
-
r
CoA + 3-oxooctanoyl-CoA
acetyl-CoA + hexanoyl-CoA
show the reaction diagram
Q64428
-
-
-
?
CoA + 3-oxooctanoyl-CoA
acetyl-CoA + hexanoyl-CoA
show the reaction diagram
Q8VCH0, Q921H8
-
-
-
?
CoA + 3-oxopalmitoyl-CoA
acetyl-CoA + tetradecanoyl-CoA
show the reaction diagram
-
-
-
-
-
CoA + 3-oxopalmitoyl-CoA
acetyl-CoA + tetradecanoyl-CoA
show the reaction diagram
-
-
-
-
?
CoA + 3-oxopentanoyl-CoA
acetyl-CoA + propanoyl-CoA
show the reaction diagram
-
-
-
-
-
CoA + 3-oxopentanoyl-CoA
acetyl-CoA + propanoyl-CoA
show the reaction diagram
-
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
?
dodecanoyl-CoA + H2O
dodecanoate + CoA
show the reaction diagram
-
acetyl-CoA hydrolase activity
-
-
?
Palmitoyl-CoA + H2O
Palmitate + CoA
show the reaction diagram
-
acetyl-CoA hydrolase activity
-
-
?
propionyl-CoA + H2O
propionate + CoA
show the reaction diagram
-
acetyl-CoA hydrolase activity
-
-
?
hexanoyl-CoA + H2O
hexanoate + CoA
show the reaction diagram
-
acetyl-CoA hydrolase activity
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
low activity with acetyl-CoA
-
-
-
additional information
?
-
-
3-oxoacyl-CoA homologues from acetoacetyl to 3-oxopalmitoyl-CoA
-
-
-
additional information
?
-
-
low activity with hexanoyl-CoA, low activity with myristoyl-CoA
-
-
-
additional information
?
-
-
low activity with myristoyl-CoA
-
-
-
additional information
?
-
-
low activity with butyryl-CoA
-
-
-
additional information
?
-
-
low activity with butyryl-CoA
-
-
-
additional information
?
-
-
acetoacetyl-CoA is a poor substrate
-
-
-
additional information
?
-
-
highest activity with medium- and long-chain 3-oxoacyl-CoA substrates, but also shows significant activity with acetoacetyl-CoA (20-30% of the optimum with 3-oxohexanoyl-CoA)
-
-
-
additional information
?
-
-
activity of the enzyme towards 3-oxoacy-CoAs increased with increasing chain length of the substrate
-
-
-
additional information
?
-
-
3-oxoacyl-coenzyme A derivatives containing 4 to 16 carbons
-
-
-
additional information
?
-
-
active with all 3-oxoacyl-CoAs (C4-C10) tested
-
-
-
additional information
?
-
-
thiolase A and B possess virtually the same substrate specificity
-
-
-
additional information
?
-
-
highest activities with medium-chain substrates
-
-
-
additional information
?
-
-
acts on 3-oxoacyl-CoA compounds of various chain lengths
-
-
-
additional information
?
-
P27796
the active site of thiolase can also catalyse the synthesis of acetyl-Co from two molecules of acetyl-CoA
-
-
-
additional information
?
-
-
key enzyme involved in fatty acid oxidation
-
-
-
additional information
?
-
Q66Q58, -
sterol carrier protein 2/3-oxoacyl-CoA thiolase is involved in trafficing of sterols and oxidation of branched-chain fatty acids
-
-
-
additional information
?
-
-
first enzyme of the most common biosynthetic pathway for polyhydroxyalkanoates, overview
-
-
-
additional information
?
-
-
the enzyme is involved in fatty acid beta-oxidation
-
-
-
additional information
?
-
Q56WD9
the peroxisomal isozyme is a biodegradative type 1 thiolase showing potential for redox control of peroxisomal fatty acid beta-oxidation, KAT activity in peroxisomes is influenced by a disulfide/dithiol change linking fatty acid beta-oxidation, overview
-
-
-
additional information
?
-
-
analysis of the substrate chain length specificity of the enzyme, high preference for acetyl-CoA
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5-methyl-3-oxo-4-hexenoyl-CoA + CoA
3-methylcrotonyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
?
7-methyl-3-oxo-6-octenoyl-CoA + CoA
5-methylhex-4-enoyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
?
acetyl-CoA + H2O
acetate + CoA
show the reaction diagram
-
-
-
-
r
acetyl-CoA + H2O
acetate + CoA
show the reaction diagram
-
3-ketoacyl-CoA thiolase activity
-
-
?
acyl-CoA + acetyl-CoA
CoA + 3-oxoacyl-CoA
show the reaction diagram
-
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
Q64428
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
enzyme catalyses the last step in the beta-oxidation cycle
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
enzyme catalyses the last step in the beta-oxidation cycle
-
-
r
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
enzyme catalyses the last step in the beta-oxidation cycle
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
P27796
enzyme catalyses the last step in the beta-oxidation cycle
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
enzyme catalyses the last step in the beta-oxidation cycle
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
Q56WD9
metabolism in the peroxisome influences metabolism in the lipid body
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
enzyme catalyses step of fatty acid beta-oxidation
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
enzyme catalyses step of fatty acid beta-oxidation
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
Q56WD9
enzyme catalyses step of fatty acid beta-oxidation
-
-
-
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
-
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-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
Rattus norvegicus Wistar
-
-
-
-
-
additional information
?
-
-
key enzyme involved in fatty acid oxidation
-
-
-
additional information
?
-
Q66Q58, -
sterol carrier protein 2/3-oxoacyl-CoA thiolase is involved in trafficing of sterols and oxidation of branched-chain fatty acids
-
-
-
additional information
?
-
-
first enzyme of the most common biosynthetic pathway for polyhydroxyalkanoates, overview
-
-
-
additional information
?
-
-
the enzyme is involved in fatty acid beta-oxidation
-
-
-
additional information
?
-
Q56WD9
the peroxisomal isozyme is a biodegradative type 1 thiolase showing potential for redox control of peroxisomal fatty acid beta-oxidation, KAT activity in peroxisomes is influenced by a disulfide/dithiol change linking fatty acid beta-oxidation, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
activates
Mg2+
-
activates
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(1R',4S',6R')-(+)-2-[(1-methyl-1H-imidazol-4-yl)sulfonyl]-N-[4-(propan-2-yloxy)phenyl]-2-azabicyclo[2.2.2]octane-6-carboxamide
-
selective over other human ELOVL sub-types, good microsomal stability
(1R',4S',6R')-(+/-)-2-(butylsulfonyl)-N-[4-(propan-2-yloxy)phenyl]-2-azabicyclo[2.2.2]octane-6-carboxamide
-
racemic mixture of endo-isomers, the exo isomers are inactive
(1R',4S',6R')-(+/-)-2-(phenylsulfonyl)-N-[4-(propan-2-yloxy)phenyl]-2-azabicyclo[2.2.2]octane-6-carboxamide
-
racemic mixture of endo-isomers, the exo isomers are inactive
(1R',4S',6R')-(+/-)-N-[4-(propan-2-yloxy)phenyl]-2-(thiophen-3-ylsulfonyl)-2-azabicyclo[2.2.2]octane-6-carboxamide
-
racemic mixture of endo-isomers, the exo isomers are inactive
3-(phenylsulfonyl)-N-[4-(propan-2-yl)phenyl]-8-azabicyclo[3.2.1]octane-8-carboxamide
-
-
3-Oxooctanoyl-CoA
-
-
3-[1-(4-chlorophenyl)-5-methyl-3-oxo-2,3-dihydro-1H-pyrazol-4-yl]-6,6-dimethyl-1-phenyl-3-(trifluoromethyl)-3,5,6,7-tetrahydro-1H-indole-2,4-dione
-
-
4-Bromo-2-octenoic acid
-
-
4-fluoro-N-[[2-oxo-6-(1H-pyrazol-1-yl)-4-(trifluoromethyl)-1,4-dihydro-2H-3,1-benzoxazin-4-yl]methyl]benzamide
Q9H5J4
-
4-fluoro-N-[[2-oxo-6-(1H-pyrazol-4-yl)-4-(trifluoromethyl)-1,4-dihydro-2H-3,1-benzoxazin-4-yl]methyl]benzamide
Q9H5J4
-
4-fluoro-N-[[2-oxo-6-(1H-pyrazol-5-yl)-4-(trifluoromethyl)-1,4-dihydro-2H-3,1-benzoxazin-4-yl]methyl]benzamide
Q9H5J4
the S-isomer shows potent and selective inhibitory activity toward human ELOVL6
4-[4-[6,6-dimethyl-2,4-dioxo-1-phenyl-3-(trifluoromethyl)-2,3,4,5,6,7-hexahydro-1H-indol-3-yl]-5-methyl-3-oxo-2,3-dihydro-1H-pyrazol-1-yl]benzonitrile
-
-
6,6-dimethyl-3-(5-methyl-3-oxo-1-phenyl-2,3-dihydro-1H-pyrazol-4-yl)-1-phenyl-3-(trifluoromethyl)-3,5,6,7-tetrahydro-1H-indole-2,4-dione
-
-
6,6-dimethyl-3-[5-methyl-1-(4-methylphenyl)-3-oxo-2,3-dihydro-1H-pyrazol-4-yl]-1-phenyl-3-(trifluoromethyl)-3,5,6,7-tetrahydro-1H-indole-2,4-dione
-
-
6,6-dimethyl-3-[5-methyl-3-oxo-1-[4-(propan-2-yl)phenyl]-2,3-dihydro-1H-pyrazol-4-yl]-1-phenyl-3-(trifluoromethyl)-3,5,6,7-tetrahydro-1H-indole-2,4-dione
-
-
6,6-dimethyl-3-[5-methyl-3-oxo-1-[4-(trifluoromethoxy)phenyl]-2,3-dihydro-1H-pyrazol-4-yl]-1-phenyl-3-(trifluoromethyl)-3,5,6,7-tetrahydro-1H-indole-2,4-dione
-
-
6,6-dimethyl-3-[5-methyl-3-oxo-1-[4-(trifluoromethoxy)phenyl]-2,3-dihydro-1H-pyrazol-4-yl]-1-phenyl-3-(trifluoromethyl)-3,5,6,7-tetrahydro-1H-indole-2,4-dione
-
inhibitor shows sustained plasma exposure and good liver penetrability. After oral administration, it potently inhibits ELOVL6 activity in liver
acetoacetyl-CoA
-
competitive inhibition of the acetyl-CoA hydrolase activity
acetoacetyl-CoA
-
substrate inhibition at high concentrations
acetyl-CoA
-
-
acetyl-CoA
-
competitive inhibition of the 3-ketoacyl-CoA thiolase activity
anti-thiolase-antibody
-
-
-
CoA
-
inhibition of condensation
CoA
-
at concentrations above 0.025 mM
cycloate
-
treatment increases the content of alkylresorcinols biosynthesised in rye in both green and etiolated plants. The presence of cycloate also affects patterns of alkylresorcinol homologues in plants grown at 15C and 22C, very-long-side-chain compounds are less abundant, whereas both short-chain saturated and unsaturated homologues are generally accumulated. No cycloate-related effects caused by homologue pattern modifications are observed at elevated temperature
cystamine
-
10 mM, inactivation with half-life of 0.6 h
Decanoyl-CoA
-
-
iodoacetamide
-
-
long-chain 3-oxoacyl-CoA compounds
-
-
N-(4-methylphenyl)-3-(phenylsulfonyl)-8-azabicyclo[3.2.1]octane-8-carboxamide
-
lead compound
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
N-Methylmaleimide
-
-
N-[4-(1,1-difluoroethyl)phenyl]-3-(phenylsulfonyl)-8-azabicyclo[3.2.1]octane-8-carboxamide
-
-
N-[4-(1,1-difluoroethyl)phenyl]-3-(pyridin-2-ylsulfonyl)-8-azabicyclo[3.2.1]octane-8-carboxamide
-
excellent selectivity over the other human ELOVL subtypes, with IC50 above 5 microM for ELOVL1, -2, -3, and -5, selective against the hERG K+ channel
N-[[6-chloro-2-oxo-4-(trifluoromethyl)-1,4-dihydro-2H-3,1-benzoxazin-4-yl]methyl]-4-fluorobenzamide
Q9H5J4
-
NEM
-
inhibition at 1 mM in absence or presence of 0.5 mM acetyl-CoA
palmitoyl-CoA
-
up to 0.03 mM
ranolazine
-
-
Semicarbazide
-
-
trimetazidine
-
-
Tris(hydroxymethyl)aminomethane
-
-
Mg2+
-
25 mM, 20% inhibition
additional information
-
in presence of 20 mM cysteamine, full activity is maintained for more than 12 h
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
di-(2-ethylhexyl)phthalate induces the enzyme
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0018
-
3-oxodecanoyl-CoA
-
-
0.0021
-
3-oxodecanoyl-CoA
-
-
0.0093
-
3-oxododecanoyl-CoA
-
-
0.0083
-
3-Oxohexanoyl-CoA
-
-
0.028
-
3-Oxohexanoyl-CoA
-
-
0.0024
-
3-Oxooctanoyl-CoA
-
-
0.0088
-
3-Oxooctanoyl-CoA
-
-
0.059
-
3-oxopentanoyl-CoA
-
-
0.01
-
acetoacetyl-CoA
-
3-oxodecanoyl-CoA
0.01
-
acetoacetyl-CoA
-
-
0.0114
-
acetoacetyl-CoA
-
pH 7.4
0.016
-
acetoacetyl-CoA
-
-
0.017
-
acetoacetyl-CoA
-
-
0.021
-
acetoacetyl-CoA
-
pH 8.2, wild-type enzyme
0.025
-
acetoacetyl-CoA
-
pH 8.0, 65C
0.027
-
acetoacetyl-CoA
-
-
0.031
-
acetoacetyl-CoA
-
-
0.058
-
acetoacetyl-CoA
-
pH 8.2, mutant enzyme H352E
0.065
-
acetoacetyl-CoA
-
pH 8.2, mutant enzyme H352Y
0.07
-
acetoacetyl-CoA
-
pH 8.2, mutant enzyme H352A
0.079
-
acetoacetyl-CoA
-
pH 8.2, mutant enzyme H352K
0.093
-
acetoacetyl-CoA
-
-
0.394
-
acetoacetyl-CoA
-
-
0.011
-
acetyl-CoA
-
pH 8.0, 65C
0.71
-
acetyl-CoA
-
pH 7.4
0.025
-
CoA
-
pH 8.0, 65C
0.0087
-
CoA-SH
-
with acetoacetyl-CoA
additional information
-
additional information
-
-
-
additional information
-
additional information
-
overview: Km of peroxisomal and mitochondrial enzyme with various substrates
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
Km values between 0.003 and 0.007 mM with substrates having a carbon chain length from 6 to 16 carbon atoms, Km values for CoA at high and low acetoacetyl-CoA concentration
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetics
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
additional information
-
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.029
-
3-Oxooctanoyl-CoA
-
sterol carrier protein X-547
0.0022
-
acetoacetyl-CoA
-
pH 7.4, competitive versus acetyl-CoA hydrolysis
0.24
-
acetyl-CoA
-
pH 7.4, competitive versus 3-ketoacyl-CoA thiolase activity
0.02
-
CoA
-
sterol carrier protein X-547
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00022
-
(1R',4S',6R')-(+)-2-[(1-methyl-1H-imidazol-4-yl)sulfonyl]-N-[4-(propan-2-yloxy)phenyl]-2-azabicyclo[2.2.2]octane-6-carboxamide
-
pH 6.5, 37C
0.00012
-
(1R',4S',6R')-(+/-)-2-(butylsulfonyl)-N-[4-(propan-2-yloxy)phenyl]-2-azabicyclo[2.2.2]octane-6-carboxamide
-
pH 6.5, 37C
0.00007
-
(1R',4S',6R')-(+/-)-2-(phenylsulfonyl)-N-[4-(propan-2-yloxy)phenyl]-2-azabicyclo[2.2.2]octane-6-carboxamide
-
pH 6.5, 37C
0.000067
-
(1R',4S',6R')-(+/-)-N-[4-(propan-2-yloxy)phenyl]-2-(thiophen-3-ylsulfonyl)-2-azabicyclo[2.2.2]octane-6-carboxamide
-
pH 6.5, 37C
0.000032
-
3-(phenylsulfonyl)-N-[4-(propan-2-yl)phenyl]-8-azabicyclo[3.2.1]octane-8-carboxamide
-
-
0.000012
-
3-[1-(4-chlorophenyl)-5-methyl-3-oxo-2,3-dihydro-1H-pyrazol-4-yl]-6,6-dimethyl-1-phenyl-3-(trifluoromethyl)-3,5,6,7-tetrahydro-1H-indole-2,4-dione
-
-
0.000026
-
4-fluoro-N-[[2-oxo-6-(1H-pyrazol-1-yl)-4-(trifluoromethyl)-1,4-dihydro-2H-3,1-benzoxazin-4-yl]methyl]benzamide
Q9H5J4
pH 6.5, 37C
0.000022
-
4-fluoro-N-[[2-oxo-6-(1H-pyrazol-4-yl)-4-(trifluoromethyl)-1,4-dihydro-2H-3,1-benzoxazin-4-yl]methyl]benzamide
Q9H5J4
pH 6.5, 37C
0.000004
-
4-fluoro-N-[[2-oxo-6-(1H-pyrazol-5-yl)-4-(trifluoromethyl)-1,4-dihydro-2H-3,1-benzoxazin-4-yl]methyl]benzamide
Q9H5J4
pH 6.5, 37C
0.000014
-
4-[4-[6,6-dimethyl-2,4-dioxo-1-phenyl-3-(trifluoromethyl)-2,3,4,5,6,7-hexahydro-1H-indol-3-yl]-5-methyl-3-oxo-2,3-dihydro-1H-pyrazol-1-yl]benzonitrile
-
-
0.00029
-
6,6-dimethyl-3-(5-methyl-3-oxo-1-phenyl-2,3-dihydro-1H-pyrazol-4-yl)-1-phenyl-3-(trifluoromethyl)-3,5,6,7-tetrahydro-1H-indole-2,4-dione
-
-
0.0000087
-
6,6-dimethyl-3-[5-methyl-1-(4-methylphenyl)-3-oxo-2,3-dihydro-1H-pyrazol-4-yl]-1-phenyl-3-(trifluoromethyl)-3,5,6,7-tetrahydro-1H-indole-2,4-dione
-
-
0.00001
-
6,6-dimethyl-3-[5-methyl-3-oxo-1-[4-(propan-2-yl)phenyl]-2,3-dihydro-1H-pyrazol-4-yl]-1-phenyl-3-(trifluoromethyl)-3,5,6,7-tetrahydro-1H-indole-2,4-dione
-
-
0.0000089
-
6,6-dimethyl-3-[5-methyl-3-oxo-1-[4-(trifluoromethoxy)phenyl]-2,3-dihydro-1H-pyrazol-4-yl]-1-phenyl-3-(trifluoromethyl)-3,5,6,7-tetrahydro-1H-indole-2,4-dione
-
-
0.00175
-
N-(4-methylphenyl)-3-(phenylsulfonyl)-8-azabicyclo[3.2.1]octane-8-carboxamide
-
-
0.000078
-
N-[4-(1,1-difluoroethyl)phenyl]-3-(phenylsulfonyl)-8-azabicyclo[3.2.1]octane-8-carboxamide
-
-
0.000079
-
N-[4-(1,1-difluoroethyl)phenyl]-3-(pyridin-2-ylsulfonyl)-8-azabicyclo[3.2.1]octane-8-carboxamide
-
-
0.000026
-
N-[[6-chloro-2-oxo-4-(trifluoromethyl)-1,4-dihydro-2H-3,1-benzoxazin-4-yl]methyl]-4-fluorobenzamide
Q9H5J4
pH 6.5, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.543
-
-
purified enzyme, acetyl-CoA hydrolase activity
26.3
-
Q64428
-
119
-
-
thiolase A, substrate: 3-oxooctanoyl-CoA
123
-
-
thiolase B, substrate: 3-oxooctanoyl-CoA
352
-
-
substrate: acetoacetyl-CoA
1082
-
-
purified enzyme
1988
-
-
substrate: 3-oxohexadecanoyl-CoA
additional information
-
-
-
additional information
-
-
-
additional information
-
Q64428
-
additional information
-
-
-
additional information
-
-
assay method
additional information
-
-
-
additional information
-
-
assay method
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
-
-
assay at
7.6
-
-
-
8
-
-
for both reaction directions
8
-
-
assay at
8.5
-
-
pI: 8.0
additional information
-
-
pI: 4.9
additional information
-
-
higher activity in phosphate than in Tris buffer
additional information
-
-
pI: 6.4
additional information
-
-
thiolase A pI: 8.45, thiolase B pI: 8.7
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
8
-
pH 7.0: no significant activity below, pH 8.0: maximum activity
7.5
9.5
-
pH 7.5 and 9.5: 50% maximum activity, pH 6.5: no activity
7.6
8.3
-
pH 7.6: maximum activity, pH 8.3: about 75% of maximum activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
65
-
-
for both reaction directions
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.02
-
Q66Q58
-
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Q8VCH0, Q921H8
very low expression; very low expression of thiolase B
Manually annotated by BRENDA team
-
di-(2-ethylhexyl)phthalate-inducible acetyl-CoA hydrolase activity
Manually annotated by BRENDA team
Pseudomonas fragi B-0771
-
-
-
Manually annotated by BRENDA team
-
di-(2-ethylhexyl)phthalate-inducible acetyl-CoA hydrolase activity
Manually annotated by BRENDA team
Q8VCH0, Q921H8
thiolasae A is mainly expressed in liver and intestine; weak expression of thiolase B
Manually annotated by BRENDA team
-
di-(2-ethylhexyl)phthalate-inducible acetyl-CoA hydrolase activity
Manually annotated by BRENDA team
Q8VCH0, Q921H8
weak expression of thiolase B
Manually annotated by BRENDA team
-
di-(2-ethylhexyl)phthalate-inducible acetyl-CoA hydrolase activity
Manually annotated by BRENDA team
Q8VCH0, Q921H8
thiolasae A is mainly expressed in liver and intestine; thiolase B exhibits hepatic expression
Manually annotated by BRENDA team
-
di-(2-ethylhexyl)phthalate-inducible acetyl-CoA hydrolase activity
Manually annotated by BRENDA team
Q66Q58
during last larval instar
Manually annotated by BRENDA team
Q8VCH0, Q921H8
very low expression; very low expression of thiolase B
Manually annotated by BRENDA team
-
cotyledons
Manually annotated by BRENDA team
-
Pex5pM mutant CHO cells
Manually annotated by BRENDA team
Q8VCH0, Q921H8
weak expression of thiolase B
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme is synthesized in the cytosol and subsequently imported into the peroxisome
Manually annotated by BRENDA team
-
enzyme is synthesized in the cytosol and subsequently imported into the peroxisome
Manually annotated by BRENDA team
-
strain D-1ML, 83% of activity
Manually annotated by BRENDA team
-
binding to inner membrane
Manually annotated by BRENDA team
-
thiolase A from normal rat liver peroxisomes and thiolase B from livers of clofibrate-treated rats
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Leishmania mexicana (strain MHOM/GT/2001/U1103)
Leishmania mexicana (strain MHOM/GT/2001/U1103)
Leishmania mexicana (strain MHOM/GT/2001/U1103)
Leishmania mexicana (strain MHOM/GT/2001/U1103)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
75000
-
-
gel filtration
85000
-
-
thiolase A and B, gel filtration
86000
-
-
gel filtration
89000
-
-
peroxisomal enzyme, sedimentation equilibrium
90000
-
-
gel filtration, rate zonal centrifugation
98000
-
-
gel filtration
100000
-
Q56WD9
recombinant detagged enzyme, gel filtration
154000
-
-
mitochondrial enzyme, sedimentation equilibrium
168000
-
-
gel filtration, sucrose density gradient centrifugation
182000
-
-
gel filtration
200000
-
-
gel filtration
240000
-
-
multienzyme complex: EC 4.2.1.17, EC 1.1.1.35, EC 5.3.3.3, EC 5.1.2.3, EC 2.3.1.16, gel filtration
260000
-
-
multienzyme complex: EC 4.2.1.17, EC 1.1.1.35, EC 5.3.3.3, EC 5.1.2.3, EC 2.3.1.16, activity of EC 2.3.1.16 resides in the 42000 Da subunit of the tetramer, SDS-PAGE
270000
-
-
multienzyme complex: enoyl-CoA hydratase, L-3-hydroxyacyl-CoA dehydrogenase, 3-ketoacyl-CoA thiolase, 3-hydroxyacyl-CoA epimerase and DELTA3-cis-DELTA-trans-enoyl-CoA isomerase, PAGE
460000
-
Q64428
gel filtration; multifunctional enzyme: 2-enoyl-CoA hydratase, 3-ketoacyl-CoA thiolase, 3-hydroxyacyl-CoA dehydrogenase, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 50000, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE
dimer
-
2 * 43000, SDS-PAGE
dimer
-
2 * 40000, peroxisomal enzyme, SDS-PAGE; 2 * 41000, mitochondrial enzyme, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE
dimer
-
2 * 41000, SDS-PAGE, thiolase B dimer dissociates into monomer with low activity during cold inactivation, thiolase A maintains its dimeric structure
octamer
Q64428
alpha4beta4, 4 * 79000 + 4 * 51000, SDS-PAGE
tetramer
-
2 * 78000 + 2 * 42000, multienzyme complex: EC 4.2.1.17, EC 1.1.1.35, EC 5.3.3.3, EC 5.1.2.3, EC 2.3.1.16, activity of EC 2.3.1.16 resides in the 42000 Da subunit, SDS-PAGE
tetramer
-
2 * 73000 + 2 * 42000, multienzyme complex: EC 4.2.1.17, EC 1.1.1.35, EC 5.3.3.3, EC 5.1.2.3, EC 2.3.1.16, SDS-PAGE
tetramer
-
mitochondrial enzyme, 4 * 41000
tetramer
-
4 * 46000, SDS-PAGE
tetramer
-
4 * 46000, SDS-PAGE
tetramer
-
4 * 45500, SDS-PAGE
tetramer
Escherichia coli B.
-
2 * 78000 + 2 * 42000, multienzyme complex: EC 4.2.1.17, EC 1.1.1.35, EC 5.3.3.3, EC 5.1.2.3, EC 2.3.1.16, activity of EC 2.3.1.16 resides in the 42000 Da subunit, SDS-PAGE
-
dimer
Q56WD9
2 * 47000, recombinant detagged enzyme, SDS-PAGE
additional information
P28790
multifunctional enzyme is composed of 2 subunits: alpha and beta, alpha subunit exhibits 3-hydroxyacyl-CoA dehydrogenase and 2-enoyl-CoA hydratase activity, beta-subunit exhibits 3-oxoacyl-CoA thiolase activity, primary structure of genes for alpha and beta subunit
additional information
P27796
the high sequence similarity between the tetrameric and dimeric thiolases suggests that the tetrameric thiolases are assemble as a dimer of two thiolase dimers
additional information
Q56WD9
crystal structure analysis, secondary structure, the enzyme shows a combination of two similar alpha/beta domains capped with a loop domain, comparison to the structure of the enzyme from Saccharomyces cerevisiae, overview
additional information
-
enzyme interacts with the multifunctional protein that is responsible for the preceding two steps in beta-oxidation, which would allow a route for substrate channeling
additional information
Pseudomonas fragi B-0771
-
multifunctional enzyme is composed of 2 subunits: alpha and beta, alpha subunit exhibits 3-hydroxyacyl-CoA dehydrogenase and 2-enoyl-CoA hydratase activity, beta-subunit exhibits 3-oxoacyl-CoA thiolase activity, primary structure of genes for alpha and beta subunit
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
Q56WD9
processing of the peroxisomal precursor protein
side-chain modification
-
deletion of the first 35 N-terminal residues including the conserved cysteine from the cDNA of enzyme, both recombinant enzyme have comparable activity in Escherichia coli, the N-terminal targeting sequenze is not essential for proper folding and function of the enzyme
proteolytic modification
-
maturation of the enzyme involves temperature-dependent cleavage by wild-type Pex5p, regulation, overview, the precursor form of thiolase is only partially processed to the mature form in a temperature-sensitive manner in the Pex5pM mutant
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purified recombinant enzyme, hanging drop vapour diffusion method, 0.002 ml of protein solution is mixed with 0.002 ml reservoir solution containing 0.1 M TrisHCl, pH 8.5, 300 mM MgCl2, and 25% w/v polyethylene glycol 4000, X-ray diffraction structure determination and analysis at 2.1-2.4 A resolution
Q56WD9
to 1.5 A resolution. The dimeric structure exhibits a typical thiolase-like fold. Dimer formation and active site conformation appear in an open, active, reduced state
-
to 1.8 A resolution. The dimeric structure exhibits a typical thiolase-like fold. Dimer formation and active site conformation appear in an open, active, reduced state
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.6
-
-
multienzyme complex, -76C, 25% glycerol v/v, stable for months
8.1
-
-
25C, 25% glycerol v/v, stable for days
9
-
-
activity destroyed after 3 days
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
pH 8.1, 25% glycerol v/v, stable for days
65
-
-
15 min, purified enzyme, completely stable
100
-
-
15 min, purified enzyme, loss of 23% of activity
additional information
-
-
enzyme exhibits reversible cold-lability: loss of acitvity at 4C in the presence of NaCl, half-maximal inactivation in ice in 4 min
additional information
-
-
thiolase B exhibits cold-lability: loss of acitvity is more pronounced at 4C than at 30C, in the presence of KCl, thiolase A is stable under the same conditions, thiolase A exhibits higher stabiliy than thiolase B at 46C, lability of the thiolase B might be compensated for by the formation of a more stable multienzyme complex
additional information
-
-
enzyme is heat-labile
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
inactivation at Tris-HCl concentration
-
glycerol or 2-mercaptoethanol stabilizes
-
inactivation at Tris-HCl concentration
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in the absence of both cystamine and cysteamine isoform KAT2 spontaneously inactivates with a half-life
-
-20C, glycerol, several weeks
-
-76C, 0.2 M potassium phosphate, pH 6.6, 25% v/v glycerol, 10 mM 2-mercaptoethanol, stable for months
-
-80C, wild-type and mutant enzymes H352E, H352A, H352K and H352Y, stable for at least 3 months
-
-20C, 50% glycerol, stable
-
frequent freeze and thaw results in a gradual loss of activity
-
25C, 0.75 M Tris-HCl, pH 8.1, 25% v/v glycerol, 10 mM 2-mercaptoethanol, stable for days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant enzyme of KAT gene on chromosome 2 mutant
-
recombinant His-tagged truncated enzyme lacking the N-terminal peroxisomal targeting sequence of 34 amino acid residues from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis, His-tag removal by thrombin, to homogeneity
Q56WD9
general method for separation, quantitation and partial purification
-
single enzyme, no part of multienzyme complex of beta-oxidation cycle
-
multienzyme complex contains enoyl-CoA hydratase, L-3-hydroxyacyl-CoA dehydrogenase, 3-ketoacyl-CoA thiolase, 3-hydroxyacyl-CoA epimerase and DELTA3-cis-DELTA-trans-enoyl-CoA isomerase
-
multienzyme complex: 3-hydroxyacyl-coenzyme A epimerase, cis-DELTA3-trans-DELTA2-enoyl-CoA isomerase, enoyl-CoA hydratase, L-3-hydroxyacyl-CoA thiolase
-
multienzyme complex: EC 4.2.1.17, EC 1.1.1.35, EC 5.3.3.3, EC 5.1.2.3, EC 2.3.1.16
-
-
Q6TXD0
trifunctional enzyme: 2-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase/3-oxoacyl-CoA thiolase
-
general method for separation, quantitation and partial purification
-
multienzyme complex: EC 4.2.1.17, EC 1.1.1.35, EC 5.3.3.3, EC 5.1.2.3, EC 2.3.1.16
-
recombinant tagged enzyme by affinity chromatography
-
native enzyme 27.2fold from liver mitochondria preparation by 5 steps of ion exchange and hydrophobic interaction chromatography
-
thiolase A and B
-
native enzyme 386.4fold to homogeneity by anion exchange, hydrophobic interaction, and hydroxylapatite chromatography, and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression of a His-tagged truncated enzyme lacking the N-terminal peroxisomal targeting sequence of 34 amino acid residues in Escherichia coli strain BL21(DE3)
Q56WD9
expression of KAT gene on chromosome 2 mutant lacking the putative N-terminal peroxisomal targeting sequence in Escherichia coli
-
expression in Escherichia coli of a full-length and truncated version
-
expression in Saccharomyces cerevisiae
-
expression in Escherichia coli
Q6TXD0
expression in Eescherichia coli
-
DNA and amino acid sequence determination, expression analysis
-
; 3-ketoacyl-CoA thiolase A and B
Q8VCH0, Q921H8
expression in Escherichia coli
P28790
recombinant expression of tagged enzyme
-
expression in Escherichia coli
-
His-tagged wild-type and His352 mutant proteins overexpressed in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
liver X Receptor LXRalpha and sterol regulatory binding protein SREBP-1c regulate hepatic Elovl5 expression. The up-regulation of Elovl5 expression by LXR agonist is likely secondary to the induction of SREBP-1c. C18-20 polyunsaturated fatty acids repress expression of SREBP-1c and Elovl5, but when combined with LXR ligand stimulation, which increases SREBP-1c mRNA and nuclear SREBP-1c, Elovl5 mRNA levels are restored to normal
-
upregulated under nitrogen starvation
Parietochloris incisa
B8YJJ0, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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
G432R
-
identification, and DNA and amino acid sequence determination, of a truncated isozyme Pex5p mutant in SK32 CHO cells, which show retarded maturation of 3-ketoacyl-CoA thiolase and acyl-CoA oxidase, and a mislocation of catalase to the cytosol, the precursor form of thiolase is only partially processed to the mature form in a temperature-sensitive manner in the Pex5pM mutant, overview
additional information
-
T-DNA insertion, using Agrobacterium tumefaciens-mediated random mutagenesis, between the genes encoding a class 4 alcohol dehydrogenase and the 3-ketoacyl-CoA thiolase in Leptosphaeria maculans causes increased gene expression and production of the functional enzyme leading to reduced pathogenicity of the mutant fungus on Brassica napus plant cotyledons, overview
additional information
Parietochloris incisa
B8YJJ0, -
functional expression in Sacchaormyces cerevisiae confers its elongase activity on C18DELTA6 polyunsaturated fatty acid
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in situ renaturation of the enzyme from the SDS-polyacrylamide gel, after solubilization, SDS removal and denaturation with 6 M guanidine hydrochloride, overview
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
3-ketoacyl coenzyme-A thiolase inhibition could be a treatment for patients with heart failure
medicine
-
mutation in the thiolase gene causes severe health problems, such as ketoacidic attacks at the age of six months followed by severe retardation