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

BRENDA support

Literature summary extracted from

  • Gupta, S.C.; Dekker, E.E.
    Evidence for the identity and some comparative properties of alpha-ketoglutarate and 2-keto-4-hydroxyglutarate dehydrogenase activity (1980), J. Biol. Chem., 255, 1107-1112.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.105 glyoxylate 2-oxoglutarate dehydrogenase complex Escherichia coli
1.2.1.105 glyoxylate 2-oxoglutarate dehydrogenase complex Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.105 0.1
-
 2-oxoglutarate
-
 Escherichia coli
1.2.1.105 0.117
-
 2-oxoglutarate
-
 Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.105 Escherichia coli
-
-
-
1.2.1.105 Sus scrofa
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.2.1.105 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2 the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH Escherichia coli
a
1.2.1.105 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2 the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH Sus scrofa
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.1.105 heart
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.105 2-oxoglutarate + lipoamide
-
 Escherichia coli S-succinyldihydrolipoamide + CO2
-
 ?
1.2.1.105 2-oxoglutarate + lipoamide
-
 Sus scrofa S-succinyldihydrolipoamide + CO2
-
 ?
1.2.1.105 additional information
-
 Escherichia coli ?
-
 ?
1.2.1.105 additional information
-
 Sus scrofa ?
-
 ?

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.2.1.105 1.64
-
 glyoxylate
-
 Sus scrofa
1.2.1.105 1.7
-
 glyoxylate
-
 Escherichia coli