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Literature summary for 2.3.1.168 extracted from

  • Perham, R.N.
    Swinging arms and swinging domains in multifunctional emzymes: catalytic machines for multistep reactions (2000), Annu. Rev. Biochem., 69, 961-1004.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Homo sapiens 5739
-
mitochondrion
-
Saccharomyces cerevisiae 5739
-

Organism

Organism UniProt Comment 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 Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine enzyme contains 1 lipoyl residue per E2 chain of branched-chain 2-oxo acid dehydrogenase Homo sapiens CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
-
?
acetyl-CoA + dihydrolipoamide enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex Acidithiobacillus ferrooxidans CoA + S-acetyldihydrolipoamide
-
?
acetyl-CoA + dihydrolipoamide enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex Haemophilus influenzae CoA + S-acetyldihydrolipoamide
-
?
acetyl-CoA + dihydrolipoamide enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex Escherichia coli CoA + S-acetyldihydrolipoamide
-
?
acetyl-CoA + dihydrolipoamide enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex Neisseria meningitidis CoA + S-acetyldihydrolipoamide
-
?
acetyl-CoA + dihydrolipoamide enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex Azotobacter vinelandii CoA + S-acetyldihydrolipoamide
-
?
acetyl-CoA + dihydrolipoamide enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex Cupriavidus necator CoA + S-acetyldihydrolipoamide
-
?
acetyl-CoA + dihydrolipoamide enzyme contains 1 lipoyl residue per E2 chain of pyruvate dehydrogenase complex Saccharomyces cerevisiae CoA + S-acetyldihydrolipoamide
-
?
acetyl-CoA + dihydrolipoamide enzyme contains 1 lipoyl residue per E2 chain of pyruvate dehydrogenase complex Zymomonas mobilis CoA + S-acetyldihydrolipoamide
-
?
acetyl-CoA + dihydrolipoamide part of the pyruvate dehydrogenase reaction Acidithiobacillus ferrooxidans CoA + S-acetyldihydrolipoamide
-
?
acetyl-CoA + dihydrolipoamide part of the pyruvate dehydrogenase reaction Haemophilus influenzae CoA + S-acetyldihydrolipoamide
-
?
acetyl-CoA + dihydrolipoamide part of the pyruvate dehydrogenase reaction Escherichia coli CoA + S-acetyldihydrolipoamide
-
?
acetyl-CoA + dihydrolipoamide part of the pyruvate dehydrogenase reaction Homo sapiens CoA + S-acetyldihydrolipoamide
-
?
acetyl-CoA + dihydrolipoamide part of the pyruvate dehydrogenase reaction Saccharomyces cerevisiae CoA + S-acetyldihydrolipoamide
-
?
acetyl-CoA + dihydrolipoamide part of the pyruvate dehydrogenase reaction Geobacillus stearothermophilus CoA + S-acetyldihydrolipoamide
-
?
acetyl-CoA + dihydrolipoamide part of the pyruvate dehydrogenase reaction Enterococcus faecalis CoA + S-acetyldihydrolipoamide
-
?
acetyl-CoA + dihydrolipoamide part of the pyruvate dehydrogenase reaction Neisseria meningitidis CoA + S-acetyldihydrolipoamide
-
?
acetyl-CoA + dihydrolipoamide part of the pyruvate dehydrogenase reaction Azotobacter vinelandii CoA + S-acetyldihydrolipoamide
-
?
acetyl-CoA + dihydrolipoamide part of the pyruvate dehydrogenase reaction Cupriavidus necator CoA + S-acetyldihydrolipoamide
-
?
acetyl-CoA + dihydrolipoamide part of the pyruvate dehydrogenase reaction Zymomonas mobilis CoA + S-acetyldihydrolipoamide
-
?
acetyl-CoA + dihydrolipoamide enzyme contains 2 lipoyl residues per E2 chain of pyruvate dehydrogenase complex Homo sapiens CoA + S-acetyldihydrolipoamide
-
?
acetyl-CoA + dihydrolipoamide enzyme contains 2 lipoyl residues per E2 chain of pyruvate dehydrogenase complex Enterococcus faecalis CoA + S-acetyldihydrolipoamide
-
?

Subunits

Subunits Comment Organism
More 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 Escherichia coli
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 Geobacillus stearothermophilus
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 Azotobacter vinelandii
More lipoyl domains and inner core in the structure of multienzyme complex, overview Zymomonas mobilis
More C-terminus of E2 is joined to the N-terminus of E3 in the pyruvate dehydrogenase complex, subunit organization Acidithiobacillus ferrooxidans

Synonyms

Synonyms Comment Organism
More enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase Homo sapiens
More enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase Acidithiobacillus ferrooxidans
More enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase Haemophilus influenzae
More enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase Escherichia coli
More enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase Saccharomyces cerevisiae
More enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase Geobacillus stearothermophilus
More enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase Enterococcus faecalis
More enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase Neisseria meningitidis
More enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase Azotobacter vinelandii
More enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase Cupriavidus necator
More enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase Zymomonas mobilis