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

BRENDA support

Literature summary extracted from

  • Hirabayashi, T.; Harada, T.
    Inhibition of the alpha-ketoglutarate dehydrogenase complex from baker's yeast by acetaldehyde and glyoxylate (1972), Agric. Biol. Chem., 36, 1249-1251.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.105 acetaldehyde 2-oxoglutarate dehydrogenase complex Saccharomyces cerevisiae
1.2.1.105 glyoxylate 2-oxoglutarate dehydrogenase complex Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.2.1.5 mitochondrion part of alpha-ketoglutarate dehydrogenase complex Saccharomyces cerevisiae 5739
-

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.105 Saccharomyces cerevisiae
-
-
-
2.2.1.5 Saccharomyces cerevisiae
-
-
-

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 Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.105 2-oxoglutarate + lipoamide
-
Saccharomyces cerevisiae S-succinyldihydrolipoamide + CO2
-
?
2.2.1.5 2-oxoglutarate + acetaldehyde
-
Saccharomyces cerevisiae 5-hydroxy-4-oxohexanoate + CO2
-
?
2.2.1.5 2-oxoglutarate + glyoxylate
-
Saccharomyces cerevisiae 2-hydroxy-3-oxohexandioate + CO2
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.2.1.5 30
-
enzyme assay at Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.2.1.5 7
-
enzyme assay at Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
2.2.1.5 thiamine diphosphate
-
Saccharomyces cerevisiae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.2.1.105 3.3
-
glyoxylate 2-oxoglutarate dehydrogenase complex Saccharomyces cerevisiae
1.2.1.105 7.2
-
acetaldehyde 2-oxoglutarate dehydrogenase complex Saccharomyces cerevisiae