BRENDA - Enzyme Database show
show all sequences of 2.3.1.168

Swinging arms and swinging domains in multifunctional emzymes: catalytic machines for multistep reactions

Perham, R.N.; Annu. Rev. Biochem. 69, 961-1004 (2000)

Data extracted from this reference:

Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Homo sapiens
5739
-
mitochondrion
-
Saccharomyces cerevisiae
5739
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Acidithiobacillus ferrooxidans
-
-
-
Azotobacter vinelandii
-
-
-
Cupriavidus necator
-
-
-
Enterococcus faecalis
-
i.e. 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
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
enzyme contains 1 lipoyl residue per E2 chain of branched-chain 2-oxo acid dehydrogenase
644846
Homo sapiens
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
-
644846
Homo sapiens
?
acetyl-CoA + dihydrolipoamide
enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
644846
Acidithiobacillus ferrooxidans
CoA + S-acetyldihydrolipoamide
-
644846
Acidithiobacillus ferrooxidans
?
acetyl-CoA + dihydrolipoamide
enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
644846
Haemophilus influenzae
CoA + S-acetyldihydrolipoamide
-
644846
Haemophilus influenzae
?
acetyl-CoA + dihydrolipoamide
enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
644846
Escherichia coli
CoA + S-acetyldihydrolipoamide
-
644846
Escherichia coli
?
acetyl-CoA + dihydrolipoamide
enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
644846
Neisseria meningitidis
CoA + S-acetyldihydrolipoamide
-
644846
Neisseria meningitidis
?
acetyl-CoA + dihydrolipoamide
enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
644846
Azotobacter vinelandii
CoA + S-acetyldihydrolipoamide
-
644846
Azotobacter vinelandii
?
acetyl-CoA + dihydrolipoamide
enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
644846
Cupriavidus necator
CoA + S-acetyldihydrolipoamide
-
644846
Cupriavidus necator
?
acetyl-CoA + dihydrolipoamide
enzyme contains 1 lipoyl residue per E2 chain of pyruvate dehydrogenase complex
644846
Saccharomyces cerevisiae
CoA + S-acetyldihydrolipoamide
-
644846
Saccharomyces cerevisiae
?
acetyl-CoA + dihydrolipoamide
enzyme contains 1 lipoyl residue per E2 chain of pyruvate dehydrogenase complex
644846
Zymomonas mobilis
CoA + S-acetyldihydrolipoamide
-
644846
Zymomonas mobilis
?
acetyl-CoA + dihydrolipoamide
part of the pyruvate dehydrogenase reaction
644846
Acidithiobacillus ferrooxidans
CoA + S-acetyldihydrolipoamide
-
644846
Acidithiobacillus ferrooxidans
?
acetyl-CoA + dihydrolipoamide
part of the pyruvate dehydrogenase reaction
644846
Haemophilus influenzae
CoA + S-acetyldihydrolipoamide
-
644846
Haemophilus influenzae
?
acetyl-CoA + dihydrolipoamide
part of the pyruvate dehydrogenase reaction
644846
Escherichia coli
CoA + S-acetyldihydrolipoamide
-
644846
Escherichia coli
?
acetyl-CoA + dihydrolipoamide
part of the pyruvate dehydrogenase reaction
644846
Homo sapiens
CoA + S-acetyldihydrolipoamide
-
644846
Homo sapiens
?
acetyl-CoA + dihydrolipoamide
part of the pyruvate dehydrogenase reaction
644846
Saccharomyces cerevisiae
CoA + S-acetyldihydrolipoamide
-
644846
Saccharomyces cerevisiae
?
acetyl-CoA + dihydrolipoamide
part of the pyruvate dehydrogenase reaction
644846
Geobacillus stearothermophilus
CoA + S-acetyldihydrolipoamide
-
644846
Geobacillus stearothermophilus
?
acetyl-CoA + dihydrolipoamide
part of the pyruvate dehydrogenase reaction
644846
Enterococcus faecalis
CoA + S-acetyldihydrolipoamide
-
644846
Enterococcus faecalis
?
acetyl-CoA + dihydrolipoamide
part of the pyruvate dehydrogenase reaction
644846
Neisseria meningitidis
CoA + S-acetyldihydrolipoamide
-
644846
Neisseria meningitidis
?
acetyl-CoA + dihydrolipoamide
part of the pyruvate dehydrogenase reaction
644846
Azotobacter vinelandii
CoA + S-acetyldihydrolipoamide
-
644846
Azotobacter vinelandii
?
acetyl-CoA + dihydrolipoamide
part of the pyruvate dehydrogenase reaction
644846
Cupriavidus necator
CoA + S-acetyldihydrolipoamide
-
644846
Cupriavidus necator
?
acetyl-CoA + dihydrolipoamide
part of the pyruvate dehydrogenase reaction
644846
Zymomonas mobilis
CoA + S-acetyldihydrolipoamide
-
644846
Zymomonas mobilis
?
acetyl-CoA + dihydrolipoamide
enzyme contains 2 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
644846
Homo sapiens
CoA + S-acetyldihydrolipoamide
-
644846
Homo sapiens
?
acetyl-CoA + dihydrolipoamide
enzyme contains 2 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
644846
Enterococcus faecalis
CoA + S-acetyldihydrolipoamide
-
644846
Enterococcus faecalis
?
Subunits
Subunits
Commentary
Organism
More
C-terminus of E2 is joined to the N-terminus of E3 in the pyruvate dehydrogenase complex, subunit organization; lipoyl domains and inner core in the structure of multienzyme complex, overview
Acidithiobacillus ferrooxidans
More
lipoyl domains and inner core in the structure of multienzyme complex, overview
Azotobacter vinelandii
More
lipoyl domains and inner core in the structure of multienzyme complex, overview
Enterococcus faecalis
More
lipoyl domains and inner core in the structure of multienzyme complex, overview
Escherichia coli
More
lipoyl domains and inner core in the structure of multienzyme complex, overview
Geobacillus stearothermophilus
More
lipoyl domains and inner core in the structure of multienzyme complex, overview
Homo sapiens
More
lipoyl domains and inner core in the structure of multienzyme complex, overview
Zymomonas mobilis
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Homo sapiens
5739
-
mitochondrion
-
Saccharomyces cerevisiae
5739
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
enzyme contains 1 lipoyl residue per E2 chain of branched-chain 2-oxo acid dehydrogenase
644846
Homo sapiens
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
-
644846
Homo sapiens
?
acetyl-CoA + dihydrolipoamide
enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
644846
Acidithiobacillus ferrooxidans
CoA + S-acetyldihydrolipoamide
-
644846
Acidithiobacillus ferrooxidans
?
acetyl-CoA + dihydrolipoamide
enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
644846
Haemophilus influenzae
CoA + S-acetyldihydrolipoamide
-
644846
Haemophilus influenzae
?
acetyl-CoA + dihydrolipoamide
enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
644846
Escherichia coli
CoA + S-acetyldihydrolipoamide
-
644846
Escherichia coli
?
acetyl-CoA + dihydrolipoamide
enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
644846
Neisseria meningitidis
CoA + S-acetyldihydrolipoamide
-
644846
Neisseria meningitidis
?
acetyl-CoA + dihydrolipoamide
enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
644846
Azotobacter vinelandii
CoA + S-acetyldihydrolipoamide
-
644846
Azotobacter vinelandii
?
acetyl-CoA + dihydrolipoamide
enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
644846
Cupriavidus necator
CoA + S-acetyldihydrolipoamide
-
644846
Cupriavidus necator
?
acetyl-CoA + dihydrolipoamide
enzyme contains 1 lipoyl residue per E2 chain of pyruvate dehydrogenase complex
644846
Saccharomyces cerevisiae
CoA + S-acetyldihydrolipoamide
-
644846
Saccharomyces cerevisiae
?
acetyl-CoA + dihydrolipoamide
enzyme contains 1 lipoyl residue per E2 chain of pyruvate dehydrogenase complex
644846
Zymomonas mobilis
CoA + S-acetyldihydrolipoamide
-
644846
Zymomonas mobilis
?
acetyl-CoA + dihydrolipoamide
part of the pyruvate dehydrogenase reaction
644846
Acidithiobacillus ferrooxidans
CoA + S-acetyldihydrolipoamide
-
644846
Acidithiobacillus ferrooxidans
?
acetyl-CoA + dihydrolipoamide
part of the pyruvate dehydrogenase reaction
644846
Haemophilus influenzae
CoA + S-acetyldihydrolipoamide
-
644846
Haemophilus influenzae
?
acetyl-CoA + dihydrolipoamide
part of the pyruvate dehydrogenase reaction
644846
Escherichia coli
CoA + S-acetyldihydrolipoamide
-
644846
Escherichia coli
?
acetyl-CoA + dihydrolipoamide
part of the pyruvate dehydrogenase reaction
644846
Homo sapiens
CoA + S-acetyldihydrolipoamide
-
644846
Homo sapiens
?
acetyl-CoA + dihydrolipoamide
part of the pyruvate dehydrogenase reaction
644846
Saccharomyces cerevisiae
CoA + S-acetyldihydrolipoamide
-
644846
Saccharomyces cerevisiae
?
acetyl-CoA + dihydrolipoamide
part of the pyruvate dehydrogenase reaction
644846
Geobacillus stearothermophilus
CoA + S-acetyldihydrolipoamide
-
644846
Geobacillus stearothermophilus
?
acetyl-CoA + dihydrolipoamide
part of the pyruvate dehydrogenase reaction
644846
Enterococcus faecalis
CoA + S-acetyldihydrolipoamide
-
644846
Enterococcus faecalis
?
acetyl-CoA + dihydrolipoamide
part of the pyruvate dehydrogenase reaction
644846
Neisseria meningitidis
CoA + S-acetyldihydrolipoamide
-
644846
Neisseria meningitidis
?
acetyl-CoA + dihydrolipoamide
part of the pyruvate dehydrogenase reaction
644846
Azotobacter vinelandii
CoA + S-acetyldihydrolipoamide
-
644846
Azotobacter vinelandii
?
acetyl-CoA + dihydrolipoamide
part of the pyruvate dehydrogenase reaction
644846
Cupriavidus necator
CoA + S-acetyldihydrolipoamide
-
644846
Cupriavidus necator
?
acetyl-CoA + dihydrolipoamide
part of the pyruvate dehydrogenase reaction
644846
Zymomonas mobilis
CoA + S-acetyldihydrolipoamide
-
644846
Zymomonas mobilis
?
acetyl-CoA + dihydrolipoamide
enzyme contains 2 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
644846
Homo sapiens
CoA + S-acetyldihydrolipoamide
-
644846
Homo sapiens
?
acetyl-CoA + dihydrolipoamide
enzyme contains 2 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
644846
Enterococcus faecalis
CoA + S-acetyldihydrolipoamide
-
644846
Enterococcus faecalis
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
C-terminus of E2 is joined to the N-terminus of E3 in the pyruvate dehydrogenase complex, subunit organization; lipoyl domains and inner core in the structure of multienzyme complex, overview
Acidithiobacillus ferrooxidans
More
lipoyl domains and inner core in the structure of multienzyme complex, overview
Azotobacter vinelandii
More
lipoyl domains and inner core in the structure of multienzyme complex, overview
Enterococcus faecalis
More
lipoyl domains and inner core in the structure of multienzyme complex, overview
Escherichia coli
More
lipoyl domains and inner core in the structure of multienzyme complex, overview
Geobacillus stearothermophilus
More
lipoyl domains and inner core in the structure of multienzyme complex, overview
Homo sapiens
More
lipoyl domains and inner core in the structure of multienzyme complex, overview
Zymomonas mobilis
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
-
-
1
-
-
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1
1
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1
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2
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1
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1
1
1
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8
2
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1
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1
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1
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1
1
1
1
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8
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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1
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1
1
1
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2
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1
1
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1
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1
1
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2
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1
1
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644845
Ansari
Epitope mapping of the branche ...
Bos taurus, Homo sapiens
J. Immunol.
153
4754-4765
1994
-
-
1
-
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2
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2
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1
-
2
-
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2
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3
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3
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1
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2
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1
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3
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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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1
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1
1
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1
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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1
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1
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1
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3
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1
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1
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1
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3
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1
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644844
Lau
The complete cDNA sequence for ...
Homo sapiens
Biochim. Biophys. Acta
1132
319-321
1992
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1
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1
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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
-
3
-
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2
2
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2
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1
1
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2
1
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4
3
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3
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2
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1
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1
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4
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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2
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644840
Chuang
Subunit structure of the dihyd ...
Bos taurus
J. Biol. Chem.
260
13779-13786
1985
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1
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1
1
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1
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1
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644839
Chuang
Catalytic and structural prope ...
Bos taurus
J. Biol. Chem.
259
9277-9284
1984
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