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2 acetyl-CoA
CoA + acetoacetyl-CoA
reaction of EC 2.3.1.9
-
-
r
2,4-dichlorophenoxybutyric acid + acetyl-CoA
?
-
-
-
-
?
3-oxo-5,6-dehydrosuberyl-CoA + CoA
2,3-dehydroadipyl-CoA + acetyl-CoA
3-oxodecanoyl-CoA + CoA
acetyl-CoA + octanoyl-CoA
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
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-
?
5-methyl-3-oxo-4-hexenoyl-CoA + CoA
3-methylcrotonyl-CoA + acetyl-CoA
-
-
-
-
?
7-methyl-3-oxo-6-octenoyl-CoA + CoA
5-methylhex-4-enoyl-CoA + acetyl-CoA
-
-
-
-
?
acetoacetyl-CoA + CoA
2 acetyl-CoA
-
-
-
?
acetyl-CoA + H2O
acetate + CoA
acyl-CoA + acetyl-CoA
CoA + 3-oxoacyl-CoA
butyryl-CoA + H2O
butanoate + CoA
-
acetyl-CoA hydrolase activity
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
CoA + 3-oxodecanoyl-CoA
acetyl-CoA + octanoyl-CoA
CoA + 3-oxododecanoyl-CoA
acetyl-CoA + decanoyl-CoA
CoA + 3-oxoheptanoyl-CoA
acetyl-CoA + pentanoyl-CoA
-
-
-
-
r
CoA + 3-oxohexadecanoyl-CoA
acetyl-CoA + tetradecanoyl-CoA
-
-
-
-
?
CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
CoA + 3-oxolauryl-CoA
acetyl-CoA + decanoyl-CoA
CoA + 3-oxooctanoyl-CoA
acetyl-CoA + hexanoyl-CoA
CoA + 3-oxopalmitoyl-CoA
acetyl-CoA + tetradecanoyl-CoA
CoA + 3-oxopentanoyl-CoA
acetyl-CoA + propanoyl-CoA
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
coenzyme A + acetoacetyl-CoA
2 acetyl-CoA
dodecanoyl-CoA + H2O
dodecanoate + CoA
-
acetyl-CoA hydrolase activity
-
-
?
hexanoyl-CoA + H2O
hexanoate + CoA
-
acetyl-CoA hydrolase activity
-
-
?
palmitoyl-CoA + H2O
palmitate + CoA
-
acetyl-CoA hydrolase activity
-
-
?
propionyl-CoA + H2O
propionate + CoA
-
acetyl-CoA hydrolase activity
-
-
?
additional information
?
-
3-oxo-5,6-dehydrosuberyl-CoA + CoA
2,3-dehydroadipyl-CoA + acetyl-CoA
-
-
-
-
?
3-oxo-5,6-dehydrosuberyl-CoA + CoA
2,3-dehydroadipyl-CoA + acetyl-CoA
-
-
-
-
?
acetyl-CoA + H2O
acetate + CoA
-
3-ketoacyl-CoA thiolase activity
-
-
?
acetyl-CoA + H2O
acetate + CoA
-
best acyl-CoA substrate, acetyl-CoA hydrolase activity
-
-
?
acetyl-CoA + H2O
acetate + CoA
-
preferred substrate, 3-ketoacyl-CoA thiolase activity
-
-
?
acetyl-CoA + H2O
acetate + CoA
-
-
-
-
r
acetyl-CoA + H2O
acetate + CoA
-
-
-
-
r
acyl-CoA + acetyl-CoA
CoA + 3-oxoacyl-CoA
-
-
-
-
?
acyl-CoA + acetyl-CoA
CoA + 3-oxoacyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
metabolism in the peroxisome influences metabolism in the lipid body
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
enzyme catalyses step of fatty acid beta-oxidation
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
r
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
two-step reaction
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
enzyme catalyses the last step in the beta-oxidation cycle
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
r
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
r
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
r
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
enzyme catalyses step of fatty acid beta-oxidation
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
r
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
enzyme catalyses the last step in the beta-oxidation cycle
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
enzyme plays important role in peroxisomal beta-oxidation, in addition the enzyme may facilitate the intraperoxysomal movement of sterols and certain other lipids
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
two-step reaction
-
r
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
enzyme catalyses the last step in the beta-oxidation cycle
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
enzyme catalyses the last step in the beta-oxidation cycle
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
enzyme catalyses step of fatty acid beta-oxidation
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
r
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
-
-
r
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
two-step reaction
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
-
enzyme catalyses the last step in the beta-oxidation cycle
-
-
r
CoA + 3-oxodecanoyl-CoA
acetyl-CoA + octanoyl-CoA
-
-
-
-
?
CoA + 3-oxodecanoyl-CoA
acetyl-CoA + octanoyl-CoA
-
-
-
-
r
CoA + 3-oxodecanoyl-CoA
acetyl-CoA + octanoyl-CoA
-
-
-
-
?
CoA + 3-oxodecanoyl-CoA
acetyl-CoA + octanoyl-CoA
-
-
-
-
?
CoA + 3-oxodecanoyl-CoA
acetyl-CoA + octanoyl-CoA
-
-
-
-
?
CoA + 3-oxodecanoyl-CoA
acetyl-CoA + octanoyl-CoA
-
-
-
-
r
CoA + 3-oxododecanoyl-CoA
acetyl-CoA + decanoyl-CoA
-
-
-
-
?
CoA + 3-oxododecanoyl-CoA
acetyl-CoA + decanoyl-CoA
-
-
-
-
?
CoA + 3-oxododecanoyl-CoA
acetyl-CoA + decanoyl-CoA
-
-
-
-
?
CoA + 3-oxododecanoyl-CoA
acetyl-CoA + decanoyl-CoA
-
-
-
-
?
CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
-
-
-
-
?
CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
-
highest activity with 3-oxohexanoyl-CoA
-
-
r
CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
-
-
-
-
?
CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
-
-
-
-
?
CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
-
highest activity with 3-oxohexanoyl-CoA
-
-
?
CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
-
-
-
-
?
CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
-
highest activity with 3-oxohexanoyl-CoA
-
-
r
CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
-
-
-
-
?
CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
-
-
-
-
r
CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
-
highest activity with 3-oxohexanoyl-CoA
-
-
r
CoA + 3-oxolauryl-CoA
acetyl-CoA + decanoyl-CoA
-
-
-
-
?
CoA + 3-oxolauryl-CoA
acetyl-CoA + decanoyl-CoA
-
-
-
-
?
CoA + 3-oxolauryl-CoA
acetyl-CoA + decanoyl-CoA
-
-
-
-
?
CoA + 3-oxooctanoyl-CoA
acetyl-CoA + hexanoyl-CoA
-
-
-
-
?
CoA + 3-oxooctanoyl-CoA
acetyl-CoA + hexanoyl-CoA
-
-
-
-
r
CoA + 3-oxooctanoyl-CoA
acetyl-CoA + hexanoyl-CoA
-
-
-
?
CoA + 3-oxooctanoyl-CoA
acetyl-CoA + hexanoyl-CoA
-
-
-
-
?
CoA + 3-oxooctanoyl-CoA
acetyl-CoA + hexanoyl-CoA
-
-
-
?
CoA + 3-oxooctanoyl-CoA
acetyl-CoA + hexanoyl-CoA
-
-
-
-
?
CoA + 3-oxooctanoyl-CoA
acetyl-CoA + hexanoyl-CoA
-
-
-
-
r
CoA + 3-oxopalmitoyl-CoA
acetyl-CoA + tetradecanoyl-CoA
-
-
-
-
?
CoA + 3-oxopalmitoyl-CoA
acetyl-CoA + tetradecanoyl-CoA
-
-
-
-
?
CoA + 3-oxopalmitoyl-CoA
acetyl-CoA + tetradecanoyl-CoA
-
-
-
-
?
CoA + 3-oxopentanoyl-CoA
acetyl-CoA + propanoyl-CoA
-
-
-
-
?
CoA + 3-oxopentanoyl-CoA
acetyl-CoA + propanoyl-CoA
-
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
-
r
coenzyme A + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
-
?
coenzyme A + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
-
?
additional information
?
-
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
?
-
-
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
?
-
-
3-oxoacyl-CoA homologues from acetoacetyl to 3-oxopalmitoyl-CoA
-
-
?
additional information
?
-
-
low activity with myristoyl-CoA
-
-
?
additional information
?
-
-
active with all 3-oxoacyl-CoAs (C4-C10) tested
-
-
?
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
?
-
-
3-oxoacyl-coenzyme A derivatives containing 4 to 16 carbons
-
-
?
additional information
?
-
-
highest activities with medium-chain substrates
-
-
?
additional information
?
-
-
highest activities with medium-chain substrates
-
-
?
additional information
?
-
-
low activity with butyryl-CoA
-
-
?
additional information
?
-
-
activity of the enzyme towards 3-oxoacy-CoAs increased with increasing chain length of the substrate
-
-
?
additional information
?
-
the enzyme catalyzes the thiolytic cleavage of medium-chain to long-chain 3-oxoacyl-CoAs to acetyl-CoA and a fatty acyl-CoA shortened by two C atom, the reaction involves residues C382, C92, and H352, overview. The enzyme can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA, EC 2.3.1.9
-
-
?
additional information
?
-
-
the enzyme catalyzes the thiolytic cleavage of medium-chain to long-chain 3-oxoacyl-CoAs to acetyl-CoA and a fatty acyl-CoA shortened by two C atom, the reaction involves residues C382, C92, and H352, overview. The enzyme can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA, EC 2.3.1.9
-
-
?
additional information
?
-
active site structure and CoA binding structure, and enzyme substrate specificity, detailed overview
-
-
?
additional information
?
-
-
active site structure and CoA binding structure, and enzyme substrate specificity, detailed overview
-
-
?
additional information
?
-
-
3-oxoacyl-CoA homologues from acetoacetyl to 3-oxopalmitoyl-CoA
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
3-oxoacyl-CoA homologues from acetoacetyl to 3-oxopalmitoyl-CoA
-
-
?
additional information
?
-
-
thiolase A and B possess virtually the same substrate specificity
-
-
?
additional information
?
-
-
key enzyme involved in fatty acid oxidation
-
-
?
additional information
?
-
-
the enzyme is involved in fatty acid beta-oxidation
-
-
?
additional information
?
-
-
analysis of the substrate chain length specificity of the enzyme, high preference for acetyl-CoA
-
-
?
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
?
-
the active site of thiolase can also catalyse the synthesis of acetyl-Co from two molecules of acetyl-CoA
-
-
?
additional information
?
-
sterol carrier protein 2/3-oxoacyl-CoA thiolase is involved in trafficing of sterols and oxidation of branched-chain fatty acids
-
-
?
additional information
?
-
-
sterol carrier protein 2/3-oxoacyl-CoA thiolase is involved in trafficing of sterols and oxidation of branched-chain fatty acids
-
-
?
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
-
-
?
additional information
?
-
-
low activity with myristoyl-CoA
-
-
?
additional information
?
-
-
low activity with butyryl-CoA
-
-
?
additional information
?
-
-
acetoacetyl-CoA is a poor substrate
-
-
?
additional information
?
-
-
acts on 3-oxoacyl-CoA compounds of various chain lengths
-
-
?
additional information
?
-
-
first enzyme of the most common biosynthetic pathway for polyhydroxyalkanoates, overview
-
-
?
additional information
?
-
-
first enzyme of the most common biosynthetic pathway for polyhydroxyalkanoates, overview
-
-
?
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(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-[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
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
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-[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
Tris(hydroxymethyl)aminomethane
-
-
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
-
competitive inhibition of the 3-ketoacyl-CoA thiolase activity
CoA
-
inhibition of condensation
CoA
-
at concentrations above 0.025 mM
N-ethylmaleimide
-
-
additional information
in presence of 20 mM cysteamine, full activity is maintained for more than 12 h
-
additional information
-
in presence of 20 mM cysteamine, full activity is maintained for more than 12 h
-
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Pramanik, A.; Pawar, S.; Antonian, E.; Schulz, H.
Five different enzymatic activities are associated with the multienzyme complex of fatty acid oxidation from Escherichia coli
J. Bacteriol.
137
469-473
1979
Escherichia coli
brenda
Pawar, S.; Schulz, H.
The structure of the multienzyme complex of fatty acid oxidation from Escherichia coli
J. Biol. Chem.
256
3894-3899
1981
Escherichia coli
brenda
Imamura, S.; Ueda, S.; Mizugaki, M.; Kawaguchi, A.
Purification of the multienzyme complex for fatty acid oxidation from Pseudomonas fragi and reconstitution of the fatty acid oxidation system
J. Biochem.
107
184-189
1990
Pseudomonas fragi
brenda
Binstock, J.F.; Schulz, H.
Fatty acid oxidation complex from Escherichia coli
Methods Enzymol.
71
403-411
1981
Escherichia coli
brenda
Sumegi, B.; Srere, P.A.
Binding of the enzymes of fatty acid beta-oxidation and some related enzymes to pig heart inner mitochondrial membrane
J. Biol. Chem.
259
8748-8752
1984
Sus scrofa
brenda
Middleton, B.
3-Oxoacyl-coenzyme A thiolases and L-3-hydroxyacyl-coenzyme A dehydrogenases
Biochem. Soc. Trans.
6
80-83
1978
Saccharomyces cerevisiae, Escherichia coli
brenda
Middleton, B.
The mitochondrial long-chain trifunctional enzyme: 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase and 3-oxoacyl-CoA thiolase
Biochem. Soc. Trans.
22
427-431
1994
Homo sapiens
brenda
Seedorf, U.; Brysch, P.; Engel, T.; Schrage, K.; Assmann, G.
Sterol carrier protein x is peroxisomal 3-oxoacyl coenzyme A thiolase with intrinsic sterol carrier and lipid transfer activity
J. Biol. Chem.
269
21277-21283
1994
Rattus norvegicus
brenda
Erdmann, R.; Kunau, W.H.
Purification and immunolocalization of the peroxisomal 3-oxoacyl-CoA thiolase from Saccharomyces cerevisiae
Yeast
10
1173-1182
1994
Saccharomyces cerevisiae
brenda
Kurihara, T.; Ueda, M.; Tanaka, A.
Peroxisomal acetoacetyl-CoA thiolase and 3-ketoacyl-CoA thiolase from an n-alkane-utilizing yeast, Candida tropicalis: purification and characterization
J. Biochem.
106
474-478
1989
Candida tropicalis
brenda
Miyazawa, S.; Osumi, T.; Hashimoto, T.
The presence of a new 3-oxoacyl-CoA thiolase in rat liver peroxisomes
Eur. J. Biochem.
103
589-596
1980
Rattus norvegicus
brenda
Miyazawa, S.; Furuta, S.; Osumi, T.; Hashimoto, T.; Ui, N.
Properties of peroxisomal 3-ketoacyl-CoA thiolase from rat liver
J. Biochem.
90
511-519
1981
Rattus norvegicus
brenda
Uchida, Y.; Izai, K.; Orii, T.; Hashimoto, T.
Novel fatty acid beta-oxidation enzymes in rat liver mitochondria. II. Purification and properties of enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein
J. Biol. Chem.
267
1034-1041
1992
Rattus norvegicus, Rattus norvegicus (Q64428)
brenda
Olesen, C.; Thomsen, K.K.; Svendsen, I.; Brandt, A.
The glyoxysomal 3-ketoacyl-CoA thiolase precursor from Brassica napus has enzymic activity when synthesized in Escherichia coli
FEBS Lett.
412
138-140
1997
Brassica napus
brenda
Middleton, B.
3-Ketoacyl-CoA thiolase of mammalian tissues
Methods Enzymol.
35 B
128-136
1975
Bos taurus, Ovis aries, Rattus norvegicus, Sus scrofa
-
brenda
Schulz, H.; Staack, H.
3-Ketoacyl-Co-A-thiolase with broad chain length specificity from pig heart muscle
Methods Enzymol.
71
389-403
1981
Sus scrofa
-
brenda
Olowe, Y.; Schulz, H.
Regulation of thiolases from pig heart. Control of fatty acid oxidation in heart
Eur. J. Biochem.
109
425-429
1980
Sus scrofa
brenda
Li, J.; Schulz, H.
4-Bromo-2-octenoic acid specifically inactivates 3-ketoacyl-CoA thiolase and thereby fatty acid oxidation in rat liver mitochondria
Biochemistry
27
5995-6000
1988
Rattus norvegicus
brenda
Feigenbaum, J.; Schulz, H.
Thiolases of Escherichia coli: purification and chain length specificities
J. Bacteriol.
122
407-411
1975
Escherichia coli
brenda
Carpenter, K.; Pollitt, R.J.; Middleton, B.
A unique, membrane-bound, multifunctional enzyme from human liver mitochondria catalysing three steps of fatty acid beta-oxidation
Biochem. Soc. Trans.
21
35S
1992
Homo sapiens
brenda
Staack, H.; Binstock, J.F.; Schulz, H.
Purification and properties of a pig heart thiolase with broad chain length specificity and comparison of thiolases from pig heart and Escherichia coli
J. Biol. Chem.
253
1827-1831
1978
Sus scrofa
brenda
Sato, S.; Hayashi, M.; Imamura, S.; Ozeki, Y.; Kawaguchi, A.
Primary structures of the genes, faoA and faoB, from Pseudomonas fragi B-0771 which encode the two subunits of the HDT multienzyme complex involved in fatty acid beta-oxidation
J. Biochem.
111
8-15
1992
Pseudomonas fragi (P28790), Pseudomonas fragi, Pseudomonas fragi B-0771 (P28790), Pseudomonas fragi B-0771
brenda
Wrensford, L.V.; Coppola, C.; Anderson, V.E.
An acyl-coenzyme A chain length dependent assay for 3-oxoacyl-coenzyme A thiolases employing acetyldithio-coenzyme A
Anal. Biochem.
192
49-54
1991
Bos taurus, Sus scrofa
brenda
Zeelen, J.P.; Wierenga, R.K.; Erdmann, R.; Kunau, W.H.
Crystallographic studies of 3-ketoacylCoA thiolase from yeast Saccharomyces cerevisiae
J. Mol. Biol.
215
211-213
1990
Saccharomyces cerevisiae
brenda
Frevert, J.; Kindl, H.
Purification of glyoxysomal acetyl-CoA acyltransferase
Hoppe-Seyler's Z. Physiol. Chem.
361
537-542
1980
Cucumis sativus
brenda
Arakawa, H.; Takiguchi, M.; Amaya, Y.; Nagata, S.; Hayashi, H.; Mori, M.
cDNA-derived amino acid sequence of rat mitochondrial 3-oxoacyl-CoA thiolase with no transient presequence: structural relationship with peroxisomal isozyme
EMBO J.
6
1361-1366
1987
Rattus norvegicus
brenda
Krahling, J.B.; Tolbert, N.E.
Peroxisomal beta-ketothiolase
Arch. Biochem. Biophys.
209
100-110
1981
Rattus norvegicus
brenda
O'Brien, W.J.; Frereman, F.E.
Evidence for a complex of three beta-oxidation enzymes in Escherichia coli: induction and localization
J. Bacteriol.
132
532-540
1977
Escherichia coli
brenda
Haywood, G.H.; Anderson, A.J.; Chu, L.; Dawes, E.A.
Characterization of two 3-ketothiolases possessing differing substrate specificities in the polyhydroxyalkanoate synthesizing organism Alcaligenes eutrophus
FEMS Microbiol. Lett.
52
91-96
1988
Cupriavidus necator
-
brenda
Oeljeklaus, S.; Fischer, K.; Gerhardt, B.
Glyoxysomal acetoacetyl-CoA thiolase and 3-oxoacyl-CoA thiolase from sunflower cotyledons
Planta
214
597-607
2002
Helianthus annuus
brenda
Mathieu, M.; Zeelen, J.P.; Pauptit, R.A.; Erdmann, R.; Kunau, W.H.; Wierenga, R.K.
The 2.8 ANG. crystal structure of peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: a five-layered alpha,beta,alpha,beta,alpha structure constructed from two core domains of identical topology
Structure
2
797-808
1994
Saccharomyces cerevisiae
brenda
Mathieu, M.; Modis, Y.; Zeelen, J.P.; Engel, C.K.; Abagyan, R.A.; Ahlberg, A.; Rasmussen, B.; Lamzin, V.S.; Kunau, W.H.; Wierenga, R.K.
The 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism
J. Mol. Biol.
273
714-728
1997
Saccharomyces cerevisiae (P27796)
brenda
Antonenkov, V.D.; Van Veldhoven, P.P.; Waelkens, E.; Mannaerts, G.P.
Comparison of the stability and substrate specificity of purified peroxisomal 3-oxoacyl-CoA thiolases A and B from rat liver
Biochim. Biophys. Acta
1437
136-141
1999
Rattus norvegicus
brenda
Kanayama, N.; Ueda, M.; Atomi, H.; Tanaka, A.
Genetic evaluation of physiological functions of thiolase isoenzymes in the n-alkane-assimilating yeast Candida tropicalis
J. Bacteriol.
180
690-698
1998
Candida tropicalis
brenda
Latruffe, N.; Nicolas-Frances, V.; Dasari, V.K.; Osumi, T.
Studies on regulation of the peroxisomal beta-oxidation at the 3-ketothiolase step: Dissection of the rat liver thiolase B gene promoter
Adv. Exp. Med. Biol.
466
253-259
1999
Rattus norvegicus
brenda
Germain, V.; Rylott, E.L.; Larson, T.R.; Sherson, S.M.; Bechtold, N.; Carde, J.P.; Bryce, J.H.; Graham, I.A.; Smith, S.M.
Requirement for 3-ketoacyl-CoA thiolase-2 in peroxisome development, fatty acid beta-oxidation and breakdown of triacylglycerol in lipid bodies of Arabidopsis seedlings
Plant J.
28
1-12
2001
Arabidopsis thaliana (Q56WD9), Arabidopsis thaliana
brenda
O'Connell, M.A.; Orr, G.; Shapiro, L.
Purification and characterization of fatty acid beta-oxidation enzymes from Caulobacter crescentus
J. Bacteriol.
172
997-1004
1990
Caulobacter vibrioides
brenda
Kim, J.H.; Park, A.K.; Cho, W.H.; Oh, S.; Lee, S.I.; Kim, H.Y.
A cDNA encoding 3-ketoacyl-CoA thiolase of soybean and its expression in Escherichia coli
Agric. Chem. Biotechnol.
46
87-91
2003
Glycine max (Q6TXD0)
-
brenda
Takeuchi, H.; Chen, J.H.; Jenkins, J.R.; Bun-Ya, M.; Turner, P.C.; Rees, H.H.
Characterization of a sterol carrier protein 2/3-oxoacyl-CoA thiolase from the cotton leafworm (Spodoptera littoralis): a lepidopteran mechanism closer to that in mammals than that in dipterans
Biochem. J.
382
93-100
2004
Spodoptera littoralis (Q66Q58), Spodoptera littoralis
brenda
Chevillard, G.; Clemencet, M.C.; Etienne, P.; Martin, P.; Pineau, T.; Latruffe, N.; Nicolas-Frances, V.
Molecular cloning, gene structure and expression profile of two mouse peroxisomal 3-ketoacyl-CoA thiolase genes
BMC Biochem.
5
3
2004
Mus musculus (Q8VCH0), Mus musculus (Q921H8), Mus musculus
brenda
Schiedel, A.C.; Oeljeklaus, S.; Minihan, P.; Dyer, J.H.
Cloning, expression, and purification of glyoxysomal 3-oxoacyl-CoA thiolase from sunflower cotyledons
Protein Expr. Purif.
33
25-33
2004
Helianthus annuus (Q6W6X6)
brenda
Zeng, J.; Li, D.
Expression and purification of His-tagged rat mitochondrial 3-ketoacyl-CoA thiolase wild-type and His352 mutant proteins
Protein Expr. Purif.
35
320-326
2004
Rattus norvegicus
brenda
Yamashita, H.; Itsuki, A.; Kimoto, M.; Hiemori, M.; Tsuji, H.
Acetate generation in rat liver mitochondria: acetyl-CoA hydrolase activity is demonstrated by 3-ketoacyl-CoA thiolase
Biochim. Biophys. Acta
1761
17-23
2006
Rattus norvegicus
brenda
Ito, R.; Morita, M.; Takahashi, N.; Shimozawa, N.; Usuda, N.; Imanaka, T.; Ito, M.
Identification of Pex5pM, and retarded maturation of 3-ketoacyl-CoA thiolase and acyl-CoA Oxidase in CHO cells expressing mutant Pex5p isoforms
J. Biochem.
138
781-790
2005
Cricetulus griseus
brenda
Sundaramoorthy, R.; Micossi, E.; Alphey, M.S.; Germain, V.; Bryce, J.H.; Smith, S.M.; Leonard, G.A.; Hunter, W.N.
The crystal structure of a plant 3-ketoacyl-CoA thiolase reveals the potential for redox control of peroxisomal fatty acid beta-oxidation
J. Mol. Biol.
359
347-357
2006
Arabidopsis thaliana (Q56WD9), Arabidopsis thaliana
brenda
Pantazaki, A.A.; Ioannou, A.K.; Kyriakidis, D.A.
A thermostable beta-ketothiolase of polyhydroxyalkanoates (PHAs) in Thermus thermophilus: purification and biochemical properties
Mol. Cell. Biochem.
269
27-36
2005
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
brenda
Elliott, C.E.; Howlett, B.J.
Overexpression of a 3-ketoacyl-CoA thiolase in Leptosphaeria maculans causes reduced pathogenicity on Brassica napus
Mol. Plant Microbe Interact.
19
588-596
2006
Leptosphaeria maculans
brenda
Fragasso, G.; Spoladore, R.; Cuko, A.; Palloshi, A.
Modulation of fatty acids oxidation in heart failure by selective pharmacological inhibition of 3-ketoacyl coenzyme-A thiolase
Curr. Clin. Pharmacol.
2
190-196
2007
Homo sapiens
brenda
Qin, Y.; Dalen, K.T.; Gustafsson, J.A.; Nebb, H.I.
Regulation of hepatic fatty acid elongase 5 by LXRalpha-SREBP-1c
Biochim. Biophys. Acta
1791
140-147
2009
Mus musculus
brenda
Sasaki, T.; Nagase, T.; Takahashi, T.; Nagumo, A.; Shimamura, K.; Miyamoto, Y.; Kitazawa, H.; Kanesaka, M.; Yoshimoto, R.; Aragane, K.; Tokita, S.; Sato, N.
Synthesis and evaluation of a novel 2-azabicyclo[2.2.2]octane class of long chain fatty acid elongase 6 (ELOVL6) inhibitors
Bioorg. Med. Chem.
17
5639-5647
2009
Homo sapiens
brenda
Green, C.D.; Ozguden-Akkoc, C.G.; Wang, Y.; Jump, D.B.; Olson, L.K.
Role of fatty acid elongases in determination of de novo synthesized monounsaturated fatty acid species
J. Lipid Res.
51
1871-1877
2010
Rattus norvegicus
brenda
Takahashi, T.; Nagase, T.; Sasaki, T.; Nagumo, A.; Shimamura, K.; Miyamoto, Y.; Kitazawa, H.; Kanesaka, M.; Yoshimoto, R.; Aragane, K.; Tokita, S.; Sato, N.
Synthesis and evaluation of a novel indoledione class of long chain fatty acid elongase 6 (ELOVL6) inhibitors
J. Med. Chem.
52
3142-3145
2009
Homo sapiens, Mus musculus
brenda
Nagase, T.; Takahashi, T.; Sasaki, T.; Nagumo, A.; Shimamura, K.; Miyamoto, Y.; Kitazawa, H.; Kanesaka, M.; Yoshimoto, R.; Aragane, K.; Tokita, S.; Sato, N.
Synthesis and biological evaluation of a novel 3-sulfonyl-8-azabicyclo[3.2.1]octane class of long chain fatty acid elongase 6 (ELOVL6) inhibitors
J. Med. Chem.
52
4111-4114
2009
Homo sapiens
brenda
Mizutani, T.; Ishikawa, S.; Nagase, T.; Takahashi, H.; Fujimura, T.; Sasaki, T.; Nagumo, A.; Shimamura, K.; Miyamoto, Y.; Kitazawa, H.; Kanesaka, M.; Yoshimoto, R.; Aragane, K.; Tokita, S.; Sato, N.
Discovery of novel benzoxazinones as potent and orally active long chain fatty acid elongase 6 inhibitors
J. Med. Chem.
52
7289-7300
2009
Homo sapiens (Q9H5J4), Homo sapiens
brenda
Iskandarov, U.; Khozin-Goldberg, I.; Ofir, R.; Cohen, Z.
Cloning and characterization of the 6 polyunsaturated fatty acid elongase from the green microalga Parietochloris incisa
Lipids
44
545-554
2009
Lobosphaera incisa (B8YJJ0), Lobosphaera incisa
brenda
Magnucka, E.G.; Suzuki, Y.; Pietr, S.J.; Kozubek, A.; Zarnowski, R.
Cycloate, an inhibitor of fatty acid elongase, modulates the metabolism of very-long-side-chain alkylresorcinols in rye seedlings
Pest Manag. Sci.
65
1065-1070
2009
Secale cereale
brenda
Teufel, R.; Mascaraque, V.; Ismail, W.; Voss, M.; Perera, J.; Eisenreich, W.; Haehnel, W.; Fuchs, G.
Bacterial phenylalanine and phenylacetate catabolic pathway revealed
Proc. Natl. Acad. Sci. USA
107
14390-14395
2010
Pseudomonas sp., Pseudomonas sp. Y2
brenda
Forster-Fromme, K.; Jendrossek, D.
Catabolism of citronellol and related acyclic terpenoids in pseudomonads
Appl. Microbiol. Biotechnol.
87
859-869
2010
Pseudomonas citronellolis
brenda
Fidaleo, M.; Arnauld, S.; Clemencet, M.C.; Chevillard, G.; Royer, M.C.; De Bruycker, M.; Wanders, R.J.; Athias, A.; Gresti, J.; Clouet, P.; Degrace, P.; Kersten, S.; Espeel, M.; Latruffe, N.; Nicolas-Frances, V.; Mandard, S.
A role for the peroxisomal 3-ketoacyl-CoA thiolase B enzyme in the control of PPAR?-mediated upregulation of SREBP-2 target genes in the liver
Biochimie
93
876-891
2011
Mus musculus
brenda
Pye, V.E.; Christensen, C.E.; Dyer, J.H.; Arent, S.; Henriksen, A.
Peroxisomal plant 3-ketoacyl-CoA thiolase structure and activity are regulated by a sensitive redox switch
J. Biol. Chem.
285
24078-24088
2010
Arabidopsis thaliana (Q56WD9), Arabidopsis thaliana, Helianthus annuus (Q6W6X6), Helianthus annuus
brenda
Jiang, T.; Zhang, X.F.; Wang, X.F.; Zhang, D.P.
Arabidopsis 3-ketoacyl-CoA thiolase-2 (KAT2), an enzyme of fatty acid beta-oxidation, is involved in ABA signal transduction
Plant Cell Physiol.
52
528-538
2011
Arabidopsis thaliana (Q56WD9), Arabidopsis thaliana
brenda
Berdichevsky, A.; Nedelcu, S.; Boulias, K.; Bishop, N.A.; Guarente, L.; Horvitz, H.R.
3-Ketoacyl thiolase delays aging of Caenorhabditis elegans and is required for lifespan extension mediated by sir-2.1
Proc. Natl. Acad. Sci. USA
107
18927-18932
2010
Caenorhabditis elegans (Q22100), Caenorhabditis elegans
brenda
Kiema, T.R.; Harijan, R.K.; Strozyk, M.; Fukao, T.; Alexson, S.E.; Wierenga, R.K.
The crystal structure of human mitochondrial 3-ketoacyl-CoA thiolase (T1): insight into the reaction mechanism of its thiolase and thioesterase activities
Acta Crystallogr. Sect. D
70
3212-3225
2014
Homo sapiens (P42765), Homo sapiens
brenda
Choi, S.; Pfleger, J.; Jeon, Y.; Yang, Z.; He, M.; Shin, H.; Sayed, D.; Astrof, S.; Abdellatif, M.
Oxoglutarate dehydrogenase and acetyl-CoA acyltransferase 2 selectively associate with H2A.Z-occupied promoters and are required for histone modifications
Biochim. Biophys. Acta
1862
194436
2019
Homo sapiens (P42765), Homo sapiens, Mus musculus (Q8BWT1), Mus musculus
brenda
Miltiadou, D.; Hager-Theodorides, A.L.; Symeou, S.; Constantinou, C.; Psifidi, A.; Banos, G.; Tzamaloukas, O.
Variants in the 3 untranslated region of the ovine acetyl-coenzyme A acyltransferase 2 gene are associated with dairy traits and exhibit differential allelic expression
J. Dairy Sci.
100
6285-6297
2017
Ovis aries (G3CH53), Ovis aries
brenda
Sah-Teli, S.; Hynönen, M.; Sulu, R.; Dalwani, S.; Schmitz, W.; Wierenga, R.; Venkatesan, R.
Insights into the stability and substrate specificity of the E. coli aerobic beta-oxidation trifunctional enzyme complex
J. Struct. Biol.
210
107494
2020
Escherichia coli (P21151), Escherichia coli
brenda
Srirangan, K.; Liu, X.; Tran, T.T.; Charles, T.C.; Moo-Young, M.; Chou, C.P.
Engineering of Escherichia coli for direct and modulated biosynthesis of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) copolymer using unrelated carbon sources
Sci. Rep.
6
36470
2016
Cupriavidus necator (Q0KBP1), Cupriavidus necator ATCC 17699 (Q0KBP1)
brenda