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
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
pyruvate fermentation to hexanol (engineered)
-
-
sitosterol degradation to androstenedione
-
-
Valine, leucine and isoleucine degradation
-
-
lipid metabolism
-
-
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
evolution
the rate-limiting steps are different in the degradative and biosynthetic thiolases. Thiolases share a structurally conserved thiolase core domain composed of topologically similar N-terminal and C-terminal subdomains and a more variable loop domain with structural features involved in the tetramerization and substrate specificity
metabolism
physiological function
additional information
the nucleophilic cysteine attacks the beta-carbon of the 3-ketoacyl-CoA and becomes covalently modified. Another cysteine, Cys382, acts first as an acid providing a proton for the leaving acetyl-CoA and next as a base abstracting a proton from the incoming CoA. The activated CoA molecule then attacks the carbonyl C atom of the acylated cysteine and the fatty acyl-CoA is released. The cysteine acting as the nucleophile is activated by a conserved histidine residue (His352)
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
reaction of EC 2.3.1.9
-
-
r
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
3-oxodecanoyl-CoA + CoA
acetyl-CoA + octanoyl-CoA
show the reaction diagram
degradation of 3-oxodecanoyl-CoA into acetyl-CoA and octanoyl-CoA by human mitochondrial 3-ketoacyl-CoA thiolase, substrate binding mode and reaction mechanism, overview
-
-
?
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
2 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
-
-
?
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
2 acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
P42765
reaction of EC 2.3.1.9
-
-
r
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
CoA + acetoacetyl-CoA
2 acetyl-CoA
show the reaction diagram
P42765
-
-
-
r
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 15°C and 22°C, 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
-
-
0.0092 - 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
14.8
acetoacetyl-CoA
Homo sapiens
P42765
pH 7.0, 25°C, recombinant wild-type enzyme, degradative reaction
1.4
acetyl-CoA
Homo sapiens
P42765
pH 7.0, 25°C, recombinant wild-type enzyme, synthesis reaction
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, 37°C
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, 37°C
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, 37°C
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, 37°C
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, 37°C
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, 37°C
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, 37°C
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, 37°C
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
25
assay at
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)
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
40000
-
2 * 40000, peroxisomal enzyme, SDS-PAGE
43000
-
2 * 43000, SDS-PAGE
45500
-
4 * 45500, SDS-PAGE
47000
2 * 47000, recombinant detagged enzyme, SDS-PAGE
50000
-
x * 50000, SDS-PAGE
51000
alpha4beta4, 4 * 79000 + 4 * 51000, SDS-PAGE
73000
-
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
75000
-
gel filtration
78000
-
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
79000
alpha4beta4, 4 * 79000 + 4 * 51000, SDS-PAGE
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
homotetramer
thiolases share a structurally conserved thiolase core domain composed of topologically similar N-terminal and C-terminal subdomains and a more variable loop domain with structural features involved in the tetramerization and substrate specificity
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 Tris–HCl, 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
-
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
-
purified recombinant wild-type and mutant enzymes in apoform and in complex with CoA, hanging drop vapour diffusion method, mixing of 0.002 ml of 4.4 mg/ml protein in 25 mM Tris-HCl pH 8.0, 1 mM DTT, with 0.002 ml of reservoir solution containing 100 mM MES, pH 6.6, or MOPS, pH 7.2, and 14-15% PEG MME 5000, equilibration against 1 ml of reservoir solution, 22°C, method optimization, X-ray diffraction structure determination and analysis at 2.0-3.3 A resolution, modeling
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6
-
multienzyme complex, -76°C, 25% glycerol v/v, stable for months
2962
8.1
-
25°C, 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
-20°C, 50% glycerol, stable
-
-20°C, glycerol, several weeks
-
-76°C, 0.2 M potassium phosphate, pH 6.6, 25% v/v glycerol, 10 mM 2-mercaptoethanol, stable for months
-
-80°C, wild-type and mutant enzymes H352E, H352A, H352K and H352Y, stable for at least 3 months
-
25°C, 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
-
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 His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, cation exchange chromatography, ultrafiltration, and gel filtration, tag cleavage by thrombin
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
-
gene ACAA2, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
His-tagged wild-type and His352 mutant proteins overexpressed in Escherichia coli
-
recombinant expression of tagged enzyme
-
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
-
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
C382A
site-directed mutagenesis
C92A
site-directed mutagenesis
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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