Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.2.1.105 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
Search for more literature for 1.2.1.105

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
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
-
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
-
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
-
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

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

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

Subunits

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

Synonyms

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

Cofactor

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