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Literature summary extracted from

  • Perham, R.N.; Jones, D.D.; Chauhan, H.J.; Howard, M.J.
    Substrate channeling in 2-oxo acid dehydrogenase multienzyme complexes (2002), Biochem. Soc. Trans., 30, 47-51.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.105 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine Escherichia coli
-
 [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
 ir
1.2.1.105 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine Geobacillus stearothermophilus
-
 [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
 ir
1.2.1.105 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine Pseudomonas putida
-
 [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
 ir
1.2.1.105 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine Azotobacter vinelandii
-
 [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
 ir
1.2.1.105 additional information Escherichia coli substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview ?
-
 ?
1.2.1.105 additional information Geobacillus stearothermophilus substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview ?
-
 ?
1.2.1.105 additional information Pseudomonas putida substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview ?
-
 ?
1.2.1.105 additional information Azotobacter vinelandii substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.105 Azotobacter vinelandii
-
 enzyme E2 is a component of the 2-oxo acid dehydrogenase multienzyme complex, consisting of enzyme components EC 1.2.4.1, EC 1.2.4.2, EC 2.3.1.12, and EC 1.8.1.4
-
1.2.1.105 Escherichia coli
-
 enzyme E2 is a component of the 2-oxo acid dehydrogenase multienzyme complex, consisting of enzyme components EC 1.2.4.2, EC 2.3.1.12, and EC 1.8.1.4
-
1.2.1.105 Geobacillus stearothermophilus
-
 enzyme E2 is a component of the 2-oxo acid dehydrogenase multienzyme complex, consisting of enzyme components EC 1.2.4.1, EC 1.2.4.2, EC 2.3.1.12, and EC 1.8.1.4
-
1.2.1.105 Pseudomonas putida
-
 enzyme E2 is a component of the 2-oxo acid dehydrogenase multienzyme complex, consisting of enzyme components EC 1.2.4.1, EC 1.2.4.2, EC 2.3.1.12, and EC 1.8.1.4
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.2.1.105 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2 substrate channeling and catalytic mechanism, active site coupling Escherichia coli
a
1.2.1.105 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2 substrate channeling and catalytic mechanism, active site coupling Geobacillus stearothermophilus
a
1.2.1.105 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2 substrate channeling and catalytic mechanism, active site coupling Pseudomonas putida
a
1.2.1.105 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2 substrate channeling and catalytic mechanism, active site coupling Azotobacter vinelandii
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.105 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
-
 Escherichia coli [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
 ir
1.2.1.105 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
-
 Geobacillus stearothermophilus [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
 ir
1.2.1.105 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
-
 Pseudomonas putida [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
 ir
1.2.1.105 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
-
 Azotobacter vinelandii [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
 ir
1.2.1.105 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine the enzyme contains a covalently attached lipoyl group, which is reductively acylated by enzyme complex component E1, EC 1.2.4.1, the enzyme component E2 catalyzes the subsequent acyl transfer to CoA Geobacillus stearothermophilus [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
 ir
1.2.1.105 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine the enzyme contains a covalently attached lipoyl group, which is reductively acylated by enzyme complex component E1, EC 1.2.4.1, the enzyme component E2 catalyzes the subsequent acyl transfer to CoA Pseudomonas putida [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
 ir
1.2.1.105 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine the enzyme contains a covalently attached lipoyl group, which is reductively acylated by enzyme complex component E1, EC 1.2.4.1, the enzyme component E2 catalyzes the subsequent acyl transfer to CoA Azotobacter vinelandii [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
 ir
1.2.1.105 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine the enzyme contains a covalently attached lipoyl group, which is reductively acylated by enzyme component E1, the enzyme component E2 catalyzes the subsequent acyl transfer to CoA Escherichia coli [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
 ir
1.2.1.105 additional information substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview Escherichia coli ?
-
 ?
1.2.1.105 additional information substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview Geobacillus stearothermophilus ?
-
 ?
1.2.1.105 additional information substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview Pseudomonas putida ?
-
 ?
1.2.1.105 additional information substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview Azotobacter vinelandii ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.105 More multienzyme complex structure Escherichia coli
1.2.1.105 More multienzyme complex structure Geobacillus stearothermophilus
1.2.1.105 More multienzyme complex structure Pseudomonas putida
1.2.1.105 More multienzyme complex structure Azotobacter vinelandii

Synonyms

EC Number Synonyms Comment Organism
1.2.1.105 2-oxoglutarate dehydrogenase
-
 Escherichia coli
1.2.1.105 2-oxoglutarate dehydrogenase
-
 Geobacillus stearothermophilus
1.2.1.105 2-oxoglutarate dehydrogenase
-
 Pseudomonas putida
1.2.1.105 2-oxoglutarate dehydrogenase
-
 Azotobacter vinelandii
1.2.1.105 E2 component of the 2-oxo acid dehydrogenase multienzyme complex Escherichia coli
1.2.1.105 E2 component of the 2-oxo acid dehydrogenase multienzyme complex Geobacillus stearothermophilus
1.2.1.105 E2 component of the 2-oxo acid dehydrogenase multienzyme complex Pseudomonas putida
1.2.1.105 E2 component of the 2-oxo acid dehydrogenase multienzyme complex Azotobacter vinelandii
1.2.1.105 OGDH
-
 Escherichia coli
1.2.1.105 OGDH
-
 Geobacillus stearothermophilus
1.2.1.105 OGDH
-
 Pseudomonas putida
1.2.1.105 OGDH
-
 Azotobacter vinelandii

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.105 NAD+
-
 Escherichia coli
1.2.1.105 NAD+
-
 Geobacillus stearothermophilus
1.2.1.105 NAD+
-
 Pseudomonas putida
1.2.1.105 NAD+
-
 Azotobacter vinelandii