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show all sequences of 2.3.1.168

Subunit and catalytic component stoichiometries of an in vitro reconstituted human pyruvate dehydrogenase complex

Brautigam, C.A.; Wynn, R.M.; Chuang, J.L.; Chuang, D.T.; J. Biol. Chem. 284, 13086-13098 (2009)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed as recombinant protein in Escherichia coli
Homo sapiens
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Purification (Commentary)
Commentary
Organism
-
Homo sapiens
Subunits
Subunits
Commentary
Organism
More
The human pyruvate dehydrogenase complex (PDC) is organized around a 60-meric dodecahedral core comprising the C-terminal domains of E2p and a noncatalytic component, E3-binding protein (E3BP), which specifically tethers E3 dimers to the PDC. Using an in vitro reconstituted PDC, densitometry, isothermal titration calorimetry, and analytical ultracentrifugation evidence provide that there are 40 copies of E2p and 20 copies of E3BP in the E2p/E3BP core. The overall maximal stoichiometry of this in vitro assembled PDC for E2p:E3BP:E1p:E3 is 40:20:40:20.
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed as recombinant protein in Escherichia coli
Homo sapiens
Purification (Commentary) (protein specific)
Commentary
Organism
-
Homo sapiens
Subunits (protein specific)
Subunits
Commentary
Organism
More
The human pyruvate dehydrogenase complex (PDC) is organized around a 60-meric dodecahedral core comprising the C-terminal domains of E2p and a noncatalytic component, E3-binding protein (E3BP), which specifically tethers E3 dimers to the PDC. Using an in vitro reconstituted PDC, densitometry, isothermal titration calorimetry, and analytical ultracentrifugation evidence provide that there are 40 copies of E2p and 20 copies of E3BP in the E2p/E3BP core. The overall maximal stoichiometry of this in vitro assembled PDC for E2p:E3BP:E1p:E3 is 40:20:40:20.
Homo sapiens
Other publictions for EC 2.3.1.168
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)
704473
Brautigam
Subunit and catalytic componen ...
Homo sapiens
J. Biol. Chem.
284
13086-13098
2009
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1
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702242
Klyuyeva
Allosteric coupling in pyruvat ...
Rattus norvegicus
Biochemistry
47
8358-8366
2008
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1
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644848
Hakozaki
Characterization of rainbow tr ...
Gallus gallus, Oncorhynchus mykiss
Comp. Biochem. Physiol. B Biochem. Mol. Biol.
132
433-442
2002
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2
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644846
Perham
Swinging arms and swinging dom ...
Acidithiobacillus ferrooxidans, Azotobacter vinelandii, Cupriavidus necator, Enterococcus faecalis, Escherichia coli, Geobacillus stearothermophilus, Haemophilus influenzae, Homo sapiens, Neisseria meningitidis, no activity in archaebacteria, no activity in Desulfovibrio africanus, Saccharomyces cerevisiae, Zymomonas mobilis
Annu. Rev. Biochem.
69
961-1004
2000
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2
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13
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22
7
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22
7
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644847
Chuang
Production of recombinant mamm ...
Bos taurus
Methods Enzymol.
324
192-200
2000
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1
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644845
Ansari
Epitope mapping of the branche ...
Bos taurus, Homo sapiens
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153
4754-4765
1994
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2
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3
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644849
Wynn
Invitro reconstitution of the ...
Bos taurus
Biochemistry
33
8962-8968
1994
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1
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1
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1
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644843
Lau
Structure of the gene encoding ...
Homo sapiens
J. Biol. Chem.
267
24090-24096
1992
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644844
Lau
The complete cDNA sequence for ...
Homo sapiens
Biochim. Biophys. Acta
1132
319-321
1992
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644842
Chuang
Maple syrup urine disease: dom ...
Bos taurus, Homo sapiens
Mol. Biol. Med.
8
49-63
1991
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2
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3
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2
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3
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644841
Hu
Subunit structure of the dihyd ...
Bos taurus
J. Biol. Chem.
261
343-349
1986
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644840
Chuang
Subunit structure of the dihyd ...
Bos taurus
J. Biol. Chem.
260
13779-13786
1985
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644839
Chuang
Catalytic and structural prope ...
Bos taurus
J. Biol. Chem.
259
9277-9284
1984
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4
5
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1
1
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