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Literature summary 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

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

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.168 Acidithiobacillus ferrooxidans
-
-
-
2.3.1.168 Azotobacter vinelandii
-
-
-
2.3.1.168 Cupriavidus necator
-
-
-
2.3.1.168 Enterococcus faecalis
-
 i.e. Enterococcus faecalis
-
2.3.1.168 Escherichia coli
-
-
-
2.3.1.168 Geobacillus stearothermophilus
-
-
-
2.3.1.168 Haemophilus influenzae
-
-
-
2.3.1.168 Homo sapiens
-
-
-
2.3.1.168 Neisseria meningitidis
-
-
-
2.3.1.168 no activity in archaebacteria
-
-
-
2.3.1.168 no activity in Desulfovibrio africanus
-
-
-
2.3.1.168 Saccharomyces cerevisiae
-
-
-
2.3.1.168 Zymomonas mobilis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.168 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
-
 ?
2.3.1.168 acetyl-CoA + dihydrolipoamide enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex Acidithiobacillus ferrooxidans CoA + S-acetyldihydrolipoamide
-
 ?
2.3.1.168 acetyl-CoA + dihydrolipoamide enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex Haemophilus influenzae CoA + S-acetyldihydrolipoamide
-
 ?
2.3.1.168 acetyl-CoA + dihydrolipoamide enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex Escherichia coli CoA + S-acetyldihydrolipoamide
-
 ?
2.3.1.168 acetyl-CoA + dihydrolipoamide enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex Neisseria meningitidis CoA + S-acetyldihydrolipoamide
-
 ?
2.3.1.168 acetyl-CoA + dihydrolipoamide enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex Azotobacter vinelandii CoA + S-acetyldihydrolipoamide
-
 ?
2.3.1.168 acetyl-CoA + dihydrolipoamide enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex Cupriavidus necator CoA + S-acetyldihydrolipoamide
-
 ?
2.3.1.168 acetyl-CoA + dihydrolipoamide enzyme contains 1 lipoyl residue per E2 chain of pyruvate dehydrogenase complex Saccharomyces cerevisiae CoA + S-acetyldihydrolipoamide
-
 ?
2.3.1.168 acetyl-CoA + dihydrolipoamide enzyme contains 1 lipoyl residue per E2 chain of pyruvate dehydrogenase complex Zymomonas mobilis CoA + S-acetyldihydrolipoamide
-
 ?
2.3.1.168 acetyl-CoA + dihydrolipoamide part of the pyruvate dehydrogenase reaction Acidithiobacillus ferrooxidans CoA + S-acetyldihydrolipoamide
-
 ?
2.3.1.168 acetyl-CoA + dihydrolipoamide part of the pyruvate dehydrogenase reaction Haemophilus influenzae CoA + S-acetyldihydrolipoamide
-
 ?
2.3.1.168 acetyl-CoA + dihydrolipoamide part of the pyruvate dehydrogenase reaction Escherichia coli CoA + S-acetyldihydrolipoamide
-
 ?
2.3.1.168 acetyl-CoA + dihydrolipoamide part of the pyruvate dehydrogenase reaction Homo sapiens CoA + S-acetyldihydrolipoamide
-
 ?
2.3.1.168 acetyl-CoA + dihydrolipoamide part of the pyruvate dehydrogenase reaction Saccharomyces cerevisiae CoA + S-acetyldihydrolipoamide
-
 ?
2.3.1.168 acetyl-CoA + dihydrolipoamide part of the pyruvate dehydrogenase reaction Geobacillus stearothermophilus CoA + S-acetyldihydrolipoamide
-
 ?
2.3.1.168 acetyl-CoA + dihydrolipoamide part of the pyruvate dehydrogenase reaction Enterococcus faecalis CoA + S-acetyldihydrolipoamide
-
 ?
2.3.1.168 acetyl-CoA + dihydrolipoamide part of the pyruvate dehydrogenase reaction Neisseria meningitidis CoA + S-acetyldihydrolipoamide
-
 ?
2.3.1.168 acetyl-CoA + dihydrolipoamide part of the pyruvate dehydrogenase reaction Azotobacter vinelandii CoA + S-acetyldihydrolipoamide
-
 ?
2.3.1.168 acetyl-CoA + dihydrolipoamide part of the pyruvate dehydrogenase reaction Cupriavidus necator CoA + S-acetyldihydrolipoamide
-
 ?
2.3.1.168 acetyl-CoA + dihydrolipoamide part of the pyruvate dehydrogenase reaction Zymomonas mobilis CoA + S-acetyldihydrolipoamide
-
 ?
2.3.1.168 acetyl-CoA + dihydrolipoamide enzyme contains 2 lipoyl residues per E2 chain of pyruvate dehydrogenase complex Homo sapiens CoA + S-acetyldihydrolipoamide
-
 ?
2.3.1.168 acetyl-CoA + dihydrolipoamide enzyme contains 2 lipoyl residues per E2 chain of pyruvate dehydrogenase complex Enterococcus faecalis CoA + S-acetyldihydrolipoamide
-
 ?

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
2.3.1.168 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
2.3.1.168 More enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase Acidithiobacillus ferrooxidans
2.3.1.168 More enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase Haemophilus influenzae
2.3.1.168 More enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase Escherichia coli
2.3.1.168 More enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase Saccharomyces cerevisiae
2.3.1.168 More enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase Geobacillus stearothermophilus
2.3.1.168 More enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase Enterococcus faecalis
2.3.1.168 More enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase Neisseria meningitidis
2.3.1.168 More enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase Azotobacter vinelandii
2.3.1.168 More enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase Cupriavidus necator
2.3.1.168 More enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase Zymomonas mobilis