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 hide
2.3.1.16
-
RECOMMENDED NAME
GeneOntology No.
acetyl-CoA C-acyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
Claisen condensation
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(4Z,7Z,10Z,13Z,16Z)-docosa-4,7,10,13,16-pentaenoate biosynthesis (6-desaturase)
-
-
(8E,10E)-dodeca-8,10-dienol biosynthesis
-
-
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 antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of unsaturated fatty acids
-
-
cholesterol degradation to androstenedione I (cholesterol oxidase)
-
-
cholesterol degradation to androstenedione II (cholesterol dehydrogenase)
-
-
docosahexaenoate biosynthesis III (6-desaturase, mammals)
-
-
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
-
-
lipid metabolism
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
pyruvate fermentation to hexanol (engineered)
-
-
sitosterol degradation to androstenedione
-
-
Valine, leucine and isoleucine degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:acetyl-CoA C-acyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9029-97-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Pex5pM mutant
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
basonym Alcaligenes eutrophus
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
male
-
-
Manually annotated by BRENDA team
B-0771
UniProt
Manually annotated by BRENDA team
gene paaJ
-
-
Manually annotated by BRENDA team
gene paaJ
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
strain HB8
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
acyl-CoA + acetyl-CoA
CoA + 3-oxoacyl-CoA
show the reaction diagram
-
-
-
-
?
butyryl-CoA + H2O
butanoate + CoA
show the reaction diagram
-
acetyl-CoA hydrolase activity
-
-
?
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-oxodecanoyl-CoA
acetyl-CoA + octanoyl-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-oxooctanoyl-CoA
acetyl-CoA + hexanoyl-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 + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
dodecanoyl-CoA + H2O
dodecanoate + CoA
show the reaction diagram
-
acetyl-CoA hydrolase activity
-
-
?
hexanoyl-CoA + H2O
hexanoate + 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
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
acyl-CoA + acetyl-CoA
CoA + 3-oxoacyl-CoA
show the reaction diagram
-
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activates
Mg2+
-
activates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
-
4-fluoro-N-[[2-oxo-6-(1H-pyrazol-4-yl)-4-(trifluoromethyl)-1,4-dihydro-2H-3,1-benzoxazin-4-yl]methyl]benzamide
-
4-fluoro-N-[[2-oxo-6-(1H-pyrazol-5-yl)-4-(trifluoromethyl)-1,4-dihydro-2H-3,1-benzoxazin-4-yl]methyl]benzamide
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
acetoacetyl-CoA
acetyl-CoA
anti-thiolase-antibody
-
-
-
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
-
-
Mg2+
-
25 mM, 20% inhibition
N-(4-methylphenyl)-3-(phenylsulfonyl)-8-azabicyclo[3.2.1]octane-8-carboxamide
-
lead compound
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
-
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
-
-
additional information
-
in presence of 20 mM cysteamine, full activity is maintained for more than 12 h
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
activates
NADH
-
activates
additional information
-
di-(2-ethylhexyl)phthalate induces the enzyme
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0018 - 0.0021
3-oxodecanoyl-CoA
0.0093
3-oxododecanoyl-CoA
-
-
0.0083 - 0.028
3-oxohexanoyl-CoA
0.0024 - 0.0088
3-oxooctanoyl-CoA
0.059
3-oxopentanoyl-CoA
-
-
0.01 - 0.394
acetoacetyl-CoA
0.011 - 0.71
acetyl-CoA
0.018 - 0.093
CoA
0.0087
CoA-SH
-
with acetoacetyl-CoA
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Helianthus annuus
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
pH 6.5, 37C
0.000032
3-(phenylsulfonyl)-N-[4-(propan-2-yl)phenyl]-8-azabicyclo[3.2.1]octane-8-carboxamide
Homo sapiens
-
-
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
Homo sapiens
-
-
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
Homo sapiens
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
Homo sapiens
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
Homo sapiens
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
Homo sapiens
-
-
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
Homo sapiens
-
-
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
Homo sapiens
-
-
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
Homo sapiens
-
-
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
Homo sapiens
-
-
0.00175
N-(4-methylphenyl)-3-(phenylsulfonyl)-8-azabicyclo[3.2.1]octane-8-carboxamide
Homo sapiens
-
-
0.000078
N-[4-(1,1-difluoroethyl)phenyl]-3-(phenylsulfonyl)-8-azabicyclo[3.2.1]octane-8-carboxamide
Homo sapiens
-
-
0.000079
N-[4-(1,1-difluoroethyl)phenyl]-3-(pyridin-2-ylsulfonyl)-8-azabicyclo[3.2.1]octane-8-carboxamide
Homo sapiens
-
-
0.000026
N-[[6-chloro-2-oxo-4-(trifluoromethyl)-1,4-dihydro-2H-3,1-benzoxazin-4-yl]methyl]-4-fluorobenzamide
Homo sapiens
Q9H5J4
pH 6.5, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.543
-
purified enzyme, acetyl-CoA hydrolase activity
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
7.6
-
-
8.5
-
pI: 8.0
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
65
-
for both reaction directions
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
di-(2-ethylhexyl)phthalate-inducible acetyl-CoA hydrolase activity
Manually annotated by BRENDA team
during last larval instar
Manually annotated by BRENDA team
very low expression; very low expression of thiolase B
Manually annotated by BRENDA team
-
cotyledons
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
Pex5pM mutant CHO cells
Manually annotated by BRENDA team
weak expression of thiolase B
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
strain D-1ML, 83% of activity
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
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)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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
ORGANISM
UNIPROT
COMMENTARY hide
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
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
gel filtration; multifunctional enzyme: 2-enoyl-CoA hydratase, 3-ketoacyl-CoA thiolase, 3-hydroxyacyl-CoA dehydrogenase, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 50000, SDS-PAGE
octamer
alpha4beta4, 4 * 79000 + 4 * 51000, SDS-PAGE
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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
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
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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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6
-
multienzyme complex, -76C, 25% glycerol v/v, stable for months
2962
8.1
-
25C, 25% glycerol v/v, stable for days
486404
9
-
activity destroyed after 3 days
486420
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol or 2-mercaptoethanol stabilizes
-
inactivation at Tris-HCl concentration
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50% glycerol, stable
-
-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
-
25C, 0.75 M Tris-HCl, pH 8.1, 25% v/v glycerol, 10 mM 2-mercaptoethanol, stable for days
-
frequent freeze and thaw results in a gradual loss of activity
-
in the absence of both cystamine and cysteamine isoform KAT2 spontaneously inactivates with a half-life
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
general method for separation, quantitation and partial purification
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
native enzyme 27.2fold from liver mitochondria preparation by 5 steps of ion exchange and hydrophobic interaction chromatography
-
native enzyme 386.4fold to homogeneity by anion exchange, hydrophobic interaction, and hydroxylapatite chromatography, and gel filtration
-
recombinant enzyme of KAT gene on chromosome 2 mutant
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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
recombinant tagged enzyme by affinity chromatography
-
single enzyme, no part of multienzyme complex of beta-oxidation cycle
-
thiolase A and B
-
trifunctional enzyme: 2-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase/3-oxoacyl-CoA thiolase
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; 3-ketoacyl-CoA thiolase A and B
DNA and amino acid sequence determination, expression analysis
-
expression in Eescherichia coli
-
expression in Escherichia coli
expression in Escherichia coli of a full-length and truncated version
-
expression in Saccharomyces cerevisiae
-
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)
expression of KAT gene on chromosome 2 mutant lacking the putative N-terminal peroxisomal targeting sequence in Escherichia coli
-
His-tagged wild-type and His352 mutant proteins overexpressed in Escherichia coli
-
recombinant expression of tagged enzyme
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EXPRESSION
ORGANISM
UNIPROT
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
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upregulated under nitrogen starvation
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
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
COMMENTARY hide
LITERATURE
medicine
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