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show all sequences of 2.3.1.9

Crystal structure and biochemical characterization of a 3-ketoacyl-CoA thiolase from Ralstoniaeutropha H16

Kim, J.; Kim, K.J.; Int. J. Biol. Macromol. 82, 425-431 (2016)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene ReH16_B0759, DNA and amino acid sequence determination and analysis, recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
Cupriavidus necator
Crystallization (Commentary)
Crystallization
Organism
purified recombinant enzyme in apoform and with bound CoA, hanging drop vapor diffusion method, mixing 0.001 ml of 40 mg/ml protein in 40 mM Tris-HCl, pH 8.0, and 5 mM 2-mercaptoethanol, with 0.001 ml of reservoir solution containing 1.0 M ammonium sulfate, 0.1 M HEPES, pH 7.25, and equilibration against 0.5 ml of reservoir solution, 20°C, 3 days, X-ray diffraction structure determination and analysis at 2.0-2.3 A resolution, molecular replacement method using the structure of Mycobacterium tuberculosis thiolase Mttt0182, PDB ID1ULQ, as a search model, structure modeling
Cupriavidus necator
Engineering
Amino acid exchange
Commentary
Organism
C377A
site-directed mutagenesis, almost inactive mutant
Cupriavidus necator
C89A
site-directed mutagenesis, almost inactive mutant
Cupriavidus necator
F156A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Cupriavidus necator
H347A
site-directed mutagenesis, almost inactive mutant
Cupriavidus necator
K17A
site-directed mutagenesis, the mutant shows 60% reduced activity compared to the wild-type enzyme
Cupriavidus necator
M124A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Cupriavidus necator
R220A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Cupriavidus necator
V231A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Cupriavidus necator
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics
Cupriavidus necator
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
CoA + acetoacetyl-CoA
Cupriavidus necator
-
2 acetyl-CoA
-
-
?
CoA + acetoacetyl-CoA
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
2 acetyl-CoA
-
-
?
additional information
Cupriavidus necator
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
?
-
-
-
additional information
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Cupriavidus necator
Q0K368
gene H16_B0759; gene H16_B0759
-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
Q0K368
gene H16_B0759; gene H16_B0759
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) to about 95% purity by nickel affinity chromatography and gel filtration
Cupriavidus necator
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
CoA + acetoacetyl-CoA
-
736252
Cupriavidus necator
2 acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
CoA substrate binding structure, overview
736252
Cupriavidus necator
2 acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
-
736252
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
2 acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
CoA substrate binding structure, overview
736252
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
2 acetyl-CoA
-
-
-
?
additional information
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
736252
Cupriavidus necator
?
-
-
-
-
additional information
the bound CoA substrate is located within the deep cleft formed by subdomains I, II, and III. The thiol group of CoA is located in the vicinity of the catalytic site for the degradation reaction, whereas,the adenosine nucleotide moiety is exposed on the surface. Unlike enzyme ReH16_A1887, that shows substantial structural changeupon the binding of CoA, the CoA-bound form of enzyme ReH16_B0759 exhibits quite similar structure to the apoform of the protein except for residual movement of Arg220. Moreover, the CoA binding mode of enzyme ReH16_B0759 is quite different from that of enzyme ReH16_A1887
736252
Cupriavidus necator
?
-
-
-
-
additional information
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
736252
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
?
-
-
-
-
additional information
the bound CoA substrate is located within the deep cleft formed by subdomains I, II, and III. The thiol group of CoA is located in the vicinity of the catalytic site for the degradation reaction, whereas,the adenosine nucleotide moiety is exposed on the surface. Unlike enzyme ReH16_A1887, that shows substantial structural changeupon the binding of CoA, the CoA-bound form of enzyme ReH16_B0759 exhibits quite similar structure to the apoform of the protein except for residual movement of Arg220. Moreover, the CoA binding mode of enzyme ReH16_B0759 is quite different from that of enzyme ReH16_A1887
736252
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
?
-
-
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
gene ReH16_B0759, DNA and amino acid sequence determination and analysis, recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
Cupriavidus necator
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant enzyme in apoform and with bound CoA, hanging drop vapor diffusion method, mixing 0.001 ml of 40 mg/ml protein in 40 mM Tris-HCl, pH 8.0, and 5 mM 2-mercaptoethanol, with 0.001 ml of reservoir solution containing 1.0 M ammonium sulfate, 0.1 M HEPES, pH 7.25, and equilibration against 0.5 ml of reservoir solution, 20°C, 3 days, X-ray diffraction structure determination and analysis at 2.0-2.3 A resolution, molecular replacement method using the structure of Mycobacterium tuberculosis thiolase Mttt0182, PDB ID1ULQ, as a search model, structure modeling
Cupriavidus necator
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C377A
site-directed mutagenesis, almost inactive mutant
Cupriavidus necator
C89A
site-directed mutagenesis, almost inactive mutant
Cupriavidus necator
F156A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Cupriavidus necator
H347A
site-directed mutagenesis, almost inactive mutant
Cupriavidus necator
K17A
site-directed mutagenesis, the mutant shows 60% reduced activity compared to the wild-type enzyme
Cupriavidus necator
M124A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Cupriavidus necator
R220A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Cupriavidus necator
V231A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Cupriavidus necator
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics
Cupriavidus necator
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
CoA + acetoacetyl-CoA
Cupriavidus necator
-
2 acetyl-CoA
-
-
?
CoA + acetoacetyl-CoA
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
2 acetyl-CoA
-
-
?
additional information
Cupriavidus necator
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
?
-
-
-
additional information
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) to about 95% purity by nickel affinity chromatography and gel filtration
Cupriavidus necator
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
CoA + acetoacetyl-CoA
-
736252
Cupriavidus necator
2 acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
CoA substrate binding structure, overview
736252
Cupriavidus necator
2 acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
-
736252
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
2 acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
CoA substrate binding structure, overview
736252
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
2 acetyl-CoA
-
-
-
?
additional information
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
736252
Cupriavidus necator
?
-
-
-
-
additional information
the bound CoA substrate is located within the deep cleft formed by subdomains I, II, and III. The thiol group of CoA is located in the vicinity of the catalytic site for the degradation reaction, whereas,the adenosine nucleotide moiety is exposed on the surface. Unlike enzyme ReH16_A1887, that shows substantial structural changeupon the binding of CoA, the CoA-bound form of enzyme ReH16_B0759 exhibits quite similar structure to the apoform of the protein except for residual movement of Arg220. Moreover, the CoA binding mode of enzyme ReH16_B0759 is quite different from that of enzyme ReH16_A1887
736252
Cupriavidus necator
?
-
-
-
-
additional information
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
736252
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
?
-
-
-
-
additional information
the bound CoA substrate is located within the deep cleft formed by subdomains I, II, and III. The thiol group of CoA is located in the vicinity of the catalytic site for the degradation reaction, whereas,the adenosine nucleotide moiety is exposed on the surface. Unlike enzyme ReH16_A1887, that shows substantial structural changeupon the binding of CoA, the CoA-bound form of enzyme ReH16_B0759 exhibits quite similar structure to the apoform of the protein except for residual movement of Arg220. Moreover, the CoA binding mode of enzyme ReH16_B0759 is quite different from that of enzyme ReH16_A1887
736252
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
?
-
-
-
-
General Information
General Information
Commentary
Organism
metabolism
the enzyme shows degradative thiolase activity catalyzing the fourth step of beta-oxidation degradative pathways by converting 3-ketoacyl-CoA to acyl-CoA
Cupriavidus necator
additional information
similar to other degradative thiolases, enzyme ReH16_B0759 functions as a dimer, and the monomer comprises three subdomains. Unlike enzyme ReH16_A1887, a substantial structural change is not observed upon the binding of the CoA substrate in enzyme ReH16_B0759. At the active site of the enzyme highly conserved residues Cys89, His347, and Cys377are located near the thiol-group of CoA
Cupriavidus necator
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the enzyme shows degradative thiolase activity catalyzing the fourth step of beta-oxidation degradative pathways by converting 3-ketoacyl-CoA to acyl-CoA
Cupriavidus necator
additional information
similar to other degradative thiolases, enzyme ReH16_B0759 functions as a dimer, and the monomer comprises three subdomains. Unlike enzyme ReH16_A1887, a substantial structural change is not observed upon the binding of the CoA substrate in enzyme ReH16_B0759. At the active site of the enzyme highly conserved residues Cys89, His347, and Cys377are located near the thiol-group of CoA
Cupriavidus necator
Other publictions for EC 2.3.1.9
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)
736252
Kim
Crystal structure and biochemi ...
Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
Int. J. Biol. Macromol.
82
425-431
2016
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8
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8
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2
2
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735372
Janardan
Structural characterization of ...
Mycolicibacterium smegmatis
Acta Crystallogr. Sect. D
71
2479-2493
2015
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1
1
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1
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2
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2
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2
1
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735404
Kim
Purification, crystallization ...
Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
Acta Crystallogr. Sect. F
71
758-762
2015
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1
1
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1
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1
2
6
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5
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1
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1
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1
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1
2
6
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1
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6
1
1
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1
1
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1
1
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1
1
735609
Kim
Crystal structure and biochemi ...
Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
Biochem. Biophys. Res. Commun.
459
547-552
2015
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1
1
7
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6
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3
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1
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8
1
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1
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1
7
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6
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1
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8
1
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2
2
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736168
Zhong
Two different subcellular-loca ...
Magnaporthe oryzae, Magnaporthe oryzae Ku80
Fungal Genet. Biol.
83
58-67
2015
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3
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4
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2
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2
2
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736542
Yun
Production of (S)-3-hydroxybut ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
J. Biotechnol.
209
23-30
2015
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1
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2
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59
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2
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-
-
-
-
-
-
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736771
Isezaki
Dictyostelium acetoacetyl-CoA ...
Dictyostelium discoideum, Dictyostelium discoideum Ax-3
Microbiology
161
1471-1484
2015
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-
-
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6
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1
2
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5
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1
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736876
Kim
Redox-switch regulatory mechan ...
Clostridium acetobutylicum
Nature Commun.
6
8410
2015
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1
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736941
Lin
Clonorchis sinensis acetoacety ...
Clonorchis sinensis
Parasit. Vectors
8
125
2015
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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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726748
Hawkins
Conversion of 4-hydroxybutyrat ...
Metallosphaera sedula, Metallosphaera sedula DSM 5348
Appl. Environ. Microbiol.
80
2536-2545
2014
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1
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4
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1
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1
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1
1
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1
1
726744
Hou
Haloarchaeal-type beta-ketothi ...
Haloferax mediterranei, Haloferax mediterranei DSM 1411
Appl. Environ. Microbiol.
79
5104-5111
2013
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1
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1
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14
2
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14
2
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1
1
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737008
Vishwakarma
-
Molecular cloning, biochemical ...
Bacopa monnieri
Plant Mol. Biol. Rep.
31
547-557
2013
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2
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1
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1
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1
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720708
Jin
Reverse genetic characterizati ...
Arabidopsis thaliana
Plant J.
70
1015-1032
2012
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6
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5
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5
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719606
Tanaka
Expression, identification and ...
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Int. J. Biol. Sci.
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2011
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1
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1
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1
1
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720134
Soto
Acetoacetyl-CoA thiolase regul ...
Medicago sativa
J. Exp. Bot.
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2011
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Ramos-Vera
Identification of missing gene ...
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706822
Thuemmler
Different clinical presentatio ...
Homo sapiens
Tohoku J. Exp. Med.
220
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2010
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4
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704027
Fujii
Molecular and functional chara ...
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2009
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7
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1
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704063
Dyer
Cloning, expression and purifi ...
Helianthus annuus
Int. J. Biol. Sci.
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706809
Battilana
The 1-deoxy-D: -xylulose 5-pho ...
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Theor. Appl. Genet.
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653-669
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Fukao
A novel single-base substituti ...
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Mol. Genet. Metab.
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2008
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Reddick
The mmgA gene from Bacillus su ...
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Biotechnol. Lett.
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Ahumada
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Characterisation of the gene f ...
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Sakurai
Kinetic and expression analyse ...
Homo sapiens
Mol. Genet. Metab.
90
370-378
2007
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9
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Haapalainen
Crystallographic and kinetic s ...
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Biochemistry
46
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Santhanam
Impairment of mitochondrial ac ...
Homo sapiens
Gut
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2007
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Treberg
Activation of liver carnitine ...
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Physiol. Biochem. Zool.
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Kursula
High resolution crystal struct ...
Escherichia coli, Homo sapiens, Zoogloea ramigera
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189-201
2005
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Pantazaki
A thermostable beta-ketothiol ...
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2005
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3
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1
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658880
Fukao
Single base substitutions at t ...
Homo sapiens
Hum. Mutat.
21
587-592
2003
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486430
Oeljeklaus
Glyoxysomal acetoacetyl-CoA th ...
Helianthus annuus
Planta
214
597-607
2002
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2
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487701
Kursula
The catalytic cycle of biosynt ...
Zoogloea ramigera
Biochemistry
41
15543-15556
2002
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1
1
2
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Hedl
Enterococcus faecalis acetoace ...
Enterococcus faecalis
J. Bacteriol.
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2002
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487703
Liu
Purification and characterizat ...
Halobacterium sp., Halobacterium sp. ZP-6
Extremophiles
6
97-102
2002
2
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1
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2
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2
4
1
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3
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486875
Lobo
A Streptomyces collinus thiola ...
Streptomyces collinus
Biochemistry
40
11955-11964
2001
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1
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1
3
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1
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1
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2
1
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3
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487699
Antonenkov
Identification, purification a ...
Rattus norvegicus
Eur. J. Biochem.
267
2981-2990
2000
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487698
Modis
A biosynthetic thiolase in com ...
Zoogloea ramigera
Structure
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486436
Kanayama
Genetic evaluation of physiolo ...
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180
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1998
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487697
Honda
Regulation of early cholestero ...
Rattus norvegicus
Hepatology
27
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1
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487694
Kanayama
Expression of acetoacetyl-CoA ...
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8
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2
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1
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Kim
Acetyl coenzyme A acetyltransf ...
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63
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1997
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3
2
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2
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1
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2
1
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2
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Heijden
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Biosynthesis of 3S-hydroxy-3-m ...
Catharanthus roseus
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32
807-812
1994
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Palmer
Biosynthetic thiolase from Zoo ...
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1
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1
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2
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487691
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Purification and characterizat ...
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1990
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1
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1
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2
1
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1
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487692
Anderson
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The reaction of acetyldithio-C ...
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1990
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4
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4
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1
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4
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4
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288676
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Peroxisomal acetoacetyl-CoA th ...
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1989
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1
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1
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1
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1
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2
1
-
2
1
-
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487688
Greenspan
The inhibition of cytoplasmic ...
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Biochem. Biophys. Res. Commun.
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1989
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1
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2
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2
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487684
Wiesenborn
Thiolase from Clostridium acet ...
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1988
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5
3
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1
1
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1
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1
1
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1
1
2
1
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1
1
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5
-
3
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1
1
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1
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1
1
2
1
-
-
-
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1
1
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487680
Davis
Biosynthetic thiolase from zoo ...
Zoogloea ramigera
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1987
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1
1
7
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1
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2
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9
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8
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1
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1
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7
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1
1
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1
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2
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9
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-
-
-
8
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487681
Davis
Biosynthetic thiolase from Zoo ...
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262
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1987
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3
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1
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1
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2
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487682
Peoples
Biosynthetic thiolase from Zoo ...
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262
97-102
1987
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1
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4
1
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1
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4
2
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487687
Suzuki
Acetoacetyl-CoA thiolase of Br ...
Bradyrhizobium japonicum
Arch. Biochem. Biophys.
254
272-281
1987
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3
4
3
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1
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1
1
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1
1
1
2
1
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2
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3
-
4
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3
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3
1
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1
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1
1
1
2
1
-
-
-
-
2
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286047
Sliwkowski
Simultaneous single-step purif ...
Clostridium kluyveri
Anal. Biochem.
141
344-347
1984
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1
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1
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2
1
1
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1
1
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1
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1
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2
1
1
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-
-
-
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487672
Hartmanis
Isolation of a selenium-contai ...
Clostridium kluyveri
Proc. Natl. Acad. Sci. USA
79
4912-4916
1982
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1
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1
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2
1
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1
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1
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1
1
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1
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2
1
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486408
Olowe
Regulation of thiolases from p ...
Sus scrofa
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425-429
1980
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2
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2
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2
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1
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1
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2
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2
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487676
Schwabe
Immunochemical aspects, molecu ...
Rattus norvegicus
Biochim. Biophys. Acta
575
112-120
1979
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1
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2
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2
1
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1
1
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2
1
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1
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2
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2
1
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487668
Nishimura
Purification and properties of ...
Zoogloea ramigera
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21-27
1978
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6
3
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2
1
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1
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1
1
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1
1
2
1
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2
2
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6
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3
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2
1
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1
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1
1
2
1
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2
2
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487674
Bloxham
Synthesis of chloromethyl keto ...
Sus scrofa
Biochem. J.
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999-1011
1978
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9
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1
1
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8
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9
8
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1
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1
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1
1
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2
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487677
Jonas
Acetyl-CoA acetyltransferase f ...
Bos taurus
Biochim. Biophys. Acta
527
379-390
1978
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6
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2
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2
1
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6
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2
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2
1
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487690
Duncombe
Molecular and catalytic proper ...
Escherichia coli
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159-170
1976
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6
1
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1
1
2
1
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6
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1
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3
1
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1
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1
1
2
1
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486410
Feigenbaum
Thiolases of Escherichia coli: ...
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407-411
1975
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1
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2
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487669
Clinkenbeard
-
Cytosolic acetoacetyl-CoA thio ...
Gallus gallus
Methods Enzymol.
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167-173
1975
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3
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3
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2
1
2
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2
1
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1
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3
1
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3
1
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1
2
1
2
1
1
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2
1
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487675
Huth
On the mechanism of ketogenesi ...
Bos taurus
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475-489
1975
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6
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1
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1
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1
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2
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1
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2
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6
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2
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487673
Middleton
The kinetic mechanism and prop ...
Rattus norvegicus
Biochem. J.
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1974
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1
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1
1
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2
1
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1
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1
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1
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2
1
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1
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1
1
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2
1
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487678
Huth
Multiple mitochondrial forms o ...
Rattus norvegicus
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1974
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2
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2
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1
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1
1
4
1
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1
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2
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2
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487670
Holland
Inactivation of pig heart thio ...
Sus scrofa
Biochemistry
12
3309-3315
1973
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7
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Clinkenbeard
Molecular and catalytic proper ...
Gallus gallus
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2275-2284
1973
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1
1
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1
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1
1
1
2
1
1
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Stern
Enzymes of ketone body metabol ...
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1
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1
1
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2
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487667
Lynen
Enzymes of fatty acid metaboli ...
Clostridium kluyveri, Sus scrofa
Biochim. Biophys. Acta
12
299-314
1953
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1
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4
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-
-
-
-
-
-
-
-
-
-
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-
-
-
-
2
-
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-
1
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4
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