BRENDA - Enzyme Database show
show all sequences of 2.8.3.5

Coenzyme A transferase. Kinetics and exchange reactions

Hersh, L.B.; Jencks, W.P.; J. Biol. Chem. 242, 3468-3480 (1967)
No PubMed abstract available

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
2,4-Dinitrophenylacetate
at pH 7.9, less inactivating activity at pH 7, acetoacetyl-CoA protects
Sus scrofa
4-nitrophenylacetate
at pH 7.9, less inactivating activity at pH 7
Sus scrofa
Acetic anhydride
-
Sus scrofa
acetoacetate
kinetics; product inhibition
Sus scrofa
acetoacetyl-CoA
EDTA, trisodium citrate and diphosphate protect, too, addition of Cu2+, Mn2+, Ca2+ or Zn2+ (decreasing order) restores inactivating activity of acetoacetyl-CoA; in the absence of succinate, cysteine restores, succinate or 0.1 M NaCl protects
Sus scrofa
Acetylimidazole
equally efficient at pH 7 and 7.9
Sus scrofa
citrate
0.167 M, weak
Sus scrofa
Glutarate
0.1 M, weak
Sus scrofa
HPO42-
0.1 M, weak
Sus scrofa
malate
0.1 M, weak
Sus scrofa
malonate
0.1 M, weak
Sus scrofa
Monovalent anions
decreasing order of effectiveness: SCN-, ClO4-, I-, Br-, Cl-, not F-
Sus scrofa
NaCl
kinetics, 24% inhibition at 10 mM
Sus scrofa
NaI
57% inhibition at 10 mM
Sus scrofa
SCN-
47% inhibition at 10 mM
Sus scrofa
SO42-
0.1 M, weak
Sus scrofa
succinate
kinetics; product inhibition
Sus scrofa
succinyl-CoA
-
Sus scrofa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic study
Sus scrofa
0.2
-
acetoacetate
cosusbstrate: succinyl-CoA, pH 8.1
Sus scrofa
0.72
-
acetoacetyl-CoA
cosusbstrate: succinate, pH 8.1
Sus scrofa
4.2
-
succinyl-CoA
cosusbstrate: acetoacetate, pH 8.1
Sus scrofa
36
-
succinate
cosusbstrate: acetoacetyl-CoA, pH 8.1
Sus scrofa
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
78000
-
gel filtration
Sus scrofa
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sus scrofa
-
-
-
Purification (Commentary)
Commentary
Organism
partial
Sus scrofa
Reaction
Reaction
Commentary
Organism
succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA
mechanism
Sus scrofa
Source Tissue
Source Tissue
Commentary
Organism
Textmining
heart
-
Sus scrofa
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
3
-
-
Sus scrofa
Storage Stability
Storage Stability
Organism
-20C, 1.4 mg protein/ml, 0.02 M potassium phosphate buffer, pH 7.4, t1/2: 9 months
Sus scrofa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
catalyzes exchange reactions in the absence of cosubstrates: succinate/succinyl-CoA and acetoacetate/acetoacetyl-CoA
645967
Sus scrofa
?
-
-
-
-
succinyl-CoA + acetoacetate
-
645967
Sus scrofa
succinate + acetoacetyl-CoA
-
645967
Sus scrofa
r
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Sus scrofa
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
25
-
1 min, inactivation at pH-values below pH 3.1 or in 0.1 M NaOH, slow loss of activity at pH 5 and pH 10.7
Sus scrofa
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
37.3
-
succinyl-CoA
pH 8.1
Sus scrofa
933
-
acetoacetyl-CoA
pH 8.1
Sus scrofa
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
8.7
-
Sus scrofa
pH Range
pH Minimum
pH Maximum
Commentary
Organism
7.1
8.7
about 50% of activity at pH 7.1, optimum at pH 8-8.7
Sus scrofa
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
3.1
-
below, 1 min at 25C, inactivation
Sus scrofa
5
-
slow loss of activity at 25C
Sus scrofa
10.7
-
slow loss of activity at 25C
Sus scrofa
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.13
-
acetoacetyl CoA
pH 8.1
Sus scrofa
0.78
-
acetoacetate
pH 8.1
Sus scrofa
1
-
succinate
pH 8.1
Sus scrofa
1.9
-
succinyl-CoA
pH 8.1
Sus scrofa
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2,4-Dinitrophenylacetate
at pH 7.9, less inactivating activity at pH 7, acetoacetyl-CoA protects
Sus scrofa
4-nitrophenylacetate
at pH 7.9, less inactivating activity at pH 7
Sus scrofa
Acetic anhydride
-
Sus scrofa
acetoacetate
kinetics; product inhibition
Sus scrofa
acetoacetyl-CoA
EDTA, trisodium citrate and diphosphate protect, too, addition of Cu2+, Mn2+, Ca2+ or Zn2+ (decreasing order) restores inactivating activity of acetoacetyl-CoA; in the absence of succinate, cysteine restores, succinate or 0.1 M NaCl protects
Sus scrofa
Acetylimidazole
equally efficient at pH 7 and 7.9
Sus scrofa
citrate
0.167 M, weak
Sus scrofa
Glutarate
0.1 M, weak
Sus scrofa
HPO42-
0.1 M, weak
Sus scrofa
malate
0.1 M, weak
Sus scrofa
malonate
0.1 M, weak
Sus scrofa
Monovalent anions
decreasing order of effectiveness: SCN-, ClO4-, I-, Br-, Cl-, not F-
Sus scrofa
NaCl
kinetics, 24% inhibition at 10 mM
Sus scrofa
NaI
57% inhibition at 10 mM
Sus scrofa
SCN-
47% inhibition at 10 mM
Sus scrofa
SO42-
0.1 M, weak
Sus scrofa
succinate
kinetics; product inhibition
Sus scrofa
succinyl-CoA
-
Sus scrofa
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.13
-
acetoacetyl CoA
pH 8.1
Sus scrofa
0.78
-
acetoacetate
pH 8.1
Sus scrofa
1
-
succinate
pH 8.1
Sus scrofa
1.9
-
succinyl-CoA
pH 8.1
Sus scrofa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic study
Sus scrofa
0.2
-
acetoacetate
cosusbstrate: succinyl-CoA, pH 8.1
Sus scrofa
0.72
-
acetoacetyl-CoA
cosusbstrate: succinate, pH 8.1
Sus scrofa
4.2
-
succinyl-CoA
cosusbstrate: acetoacetate, pH 8.1
Sus scrofa
36
-
succinate
cosusbstrate: acetoacetyl-CoA, pH 8.1
Sus scrofa
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
78000
-
gel filtration
Sus scrofa
Purification (Commentary) (protein specific)
Commentary
Organism
partial
Sus scrofa
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
heart
-
Sus scrofa
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
3
-
-
Sus scrofa
Storage Stability (protein specific)
Storage Stability
Organism
-20C, 1.4 mg protein/ml, 0.02 M potassium phosphate buffer, pH 7.4, t1/2: 9 months
Sus scrofa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
catalyzes exchange reactions in the absence of cosubstrates: succinate/succinyl-CoA and acetoacetate/acetoacetyl-CoA
645967
Sus scrofa
?
-
-
-
-
succinyl-CoA + acetoacetate
-
645967
Sus scrofa
succinate + acetoacetyl-CoA
-
645967
Sus scrofa
r
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Sus scrofa
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
25
-
1 min, inactivation at pH-values below pH 3.1 or in 0.1 M NaOH, slow loss of activity at pH 5 and pH 10.7
Sus scrofa
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
37.3
-
succinyl-CoA
pH 8.1
Sus scrofa
933
-
acetoacetyl-CoA
pH 8.1
Sus scrofa
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
8.7
-
Sus scrofa
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
7.1
8.7
about 50% of activity at pH 7.1, optimum at pH 8-8.7
Sus scrofa
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
3.1
-
below, 1 min at 25C, inactivation
Sus scrofa
5
-
slow loss of activity at 25C
Sus scrofa
10.7
-
slow loss of activity at 25C
Sus scrofa
Other publictions for EC 2.8.3.5
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
737365
Zhang
Structure of succinyl-CoA:3-ke ...
Drosophila melanogaster
Acta Crystallogr. Sect. F
69
1089-1093
2013
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1
1
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737420
Cong
Metallothionein prevents diabe ...
Mus musculus
Am. J. Physiol. Endocrinol. Metab.
304
E826-E835
2013
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1
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1
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738807
Shafqat
A structural mapping of mutati ...
Homo sapiens
J. Inherit. Metab. Dis.
36
983-987
2013
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1
1
22
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1
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22
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1
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738997
Chutoam
RpoS and oxidative stress cond ...
Burkholderia pseudomallei, Burkholderia pseudomallei K96243
Microbiol. Immunol.
57
605-615
2013
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724424
Fukao
Clinical and molecular charact ...
Homo sapiens
Biochim. Biophys. Acta
1812
619-624
2011
-
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1
-
7
-
-
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3
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2
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1
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1
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7
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2
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1
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1
1
-
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723826
Coker
The high-resolution structure ...
Sus scrofa
Acta Crystallogr. Sect. D
66
797-805
2010
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1
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1
1
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724109
Hasan
Lower succinyl-CoA:3-ketoacid- ...
Rattus norvegicus
Arch. Biochem. Biophys.
499
62-68
2010
-
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1
-
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2
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1
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2
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1
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1
1
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724277
Fraser
Catalytic role of the conforma ...
Sus scrofa
Biochemistry
49
10319-10328
2010
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1
1
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1
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703384
MacDonald
Decreased levels of metabolic ...
Homo sapiens
Diabetologia
52
1087-1091
2009
-
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1
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2
2
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703810
Bregere
Effects of age and calorie res ...
Rattus norvegicus
Free Radic. Biol. Med.
48
609-618
2009
-
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-
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2
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2
1
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3
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1
1
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2
1
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2
2
1
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1
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3
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1
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2
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3
1
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2
2
1
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1
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2
1
3
3
1
-
-
705310
Skinner
Ketone bodies inhibit the viab ...
Homo sapiens
J. Pediatr. Surg.
44
212-216
2009
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1
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4
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1
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1
1
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695186
Orii
Liver-specific silencing of th ...
Homo sapiens
Tohoku J. Exp. Med.
215
227-236
2008
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1
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705523
Bregere
Detection and characterization ...
Rattus norvegicus
Methods Enzymol.
441
339-349
2008
-
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1
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1
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1
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1
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1
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1
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1
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672216
Tammam
Identification of the cysteine ...
Sus scrofa
Biochemistry
46
10852-10863
2007
-
1
1
1
4
-
11
11
1
1
-
4
-
4
-
-
1
1
-
2
4
-
6
2
1
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6
1
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1
2
-
2
6
-
-
11
-
22
1
1
-
4
-
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2
-
3
7
-
6
2
1
-
-
6
1
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-
-
-
-
-
-
-
-
676034
Yamada
Single-base substitution at th ...
Homo sapiens
Mol. Genet. Metab.
90
291-297
2007
-
-
1
-
1
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1
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2
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1
1
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1
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Nitration of tryptophan 372 in ...
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Different localization in rat ...
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Structure of the CoA transfera ...
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Fukao
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Cloning and characterization o ...
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Neonatal hypoglycaemia in seve ...
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Lloyd
dimeric pig heart succinate-co ...
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Marcondes
Nitration of succinyl-CoA:3-ox ...
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Rochet
Productive interactions betwee ...
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Succinyl-CoA:3-ketoacid coenzy ...
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Purification and properties of ...
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Activity of 3-oxo acid CoA-tra ...
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The role of 3-oxo acid-CoA tra ...
Clupea harengus, Columba livia, Dicentrarchus labrax, Gallus gallus, Lacerta viridis, Mus musculus, Oncorhynchus mykiss, Oryctolagus cuniculus, Pleuronectes platessa, Raja clavata, Rattus norvegicus, Scomber scombrus, Scyliorhinus canicula
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Sharp
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1
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4
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645975
Fenselau
Ping-pong chromatography. A no ...
Rattus norvegicus
Biochem. Biophys. Res. Commun.
62
350-356
1975
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4
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645972
Fenselau
Comparative studies on 3-oxo a ...
Rattus norvegicus
Biochem. J.
142
619-627
1974
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645974
Fenselau
Ketone body usage by mammals. ...
Rattus norvegicus
Life Sci.
15
811-818
1974
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645978
Fenselau
Substrate specificity and mech ...
Rattus norvegicus
Biochemistry
13
3884-3889
1974
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15
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1
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6
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645968
Edwards
A simple purification of aceto ...
Sus scrofa
FEBS Lett.
37
155-158
1973
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645967
Hersh
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Sus scrofa
J. Biol. Chem.
242
3468-3480
1967
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