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EC Tree
IUBMB Comments Contains thiamine diphosphate. It is a component of the multienzyme 2-oxoglutarate dehydrogenase complex, EC 1.2.1.105, in which multiple copies of it are bound to a core of molecules of EC 2.3.1.61, dihydrolipoyllysine-residue succinyltransferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.61.
The taxonomic range for the selected organisms is: Escherichia coli The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
alpha-ketoglutarate dehydrogenase, 2-oxoglutarate dehydrogenase, kgdhc, alpha-ketoglutarate dehydrogenase complex, 2-oxoglutarate dehydrogenase complex, oxoglutarate dehydrogenase, kgdh, dhtkd1, ogdhl, ogdhc,
more
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2-oxoglutarate decarboxylase
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alpha-ketoglutarate dehydrogenase
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E1 component of the 2-oxoglutarate dehydrogenase multienzyme complex
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2-ketoglutarate dehydrogenase
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2-oxoglutarate decarboxylase
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part of the 2-oxoglutarate dehydrogenase complex
2-oxoglutarate dehydrogenase
2-oxoglutarate dehydrogenase complex
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2-oxoglutarate:lipoate oxidoreductase
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alpha-ketoglutarate dehydrogenase
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alpha-ketoglutaric acid dehydrogenase
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alpha-ketoglutaric dehydrogenase
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alpha-oxoglutarate dehydrogenase
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dehydrogenase, oxoglutarate
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ketoglutaric dehydrogenase
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oxoglutarate decarboxylase
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oxoglutarate dehydrogenase
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2-oxoglutarate dehydrogenase
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2-oxoglutarate dehydrogenase
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E1o
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E1o
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2-oxoglutarate dehydrogenase subunit of the 2-oxoglutarate dehydrogenase complex
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4)
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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
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oxidative decarboxylation
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2-oxoglutarate:[dihydrolipoyllysine-residue succinyltransferase]-lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-succinylating)
Contains thiamine diphosphate. It is a component of the multienzyme 2-oxoglutarate dehydrogenase complex, EC 1.2.1.105, in which multiple copies of it are bound to a core of molecules of EC 2.3.1.61, dihydrolipoyllysine-residue succinyltransferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.61.
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
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2-oxo-5-hexenoic acid + 2,6-dichlorophenolindophenol
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2-oxo-5-hexenoic acid + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-pent-4-enoyldihydrolipoyllysine + CO2
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2-oxo-5-hexenoic acid is not a substrate for wild-type
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2-oxoglutarate + 2,6-dichlorophenolindophenol
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2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
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2-oxovalerate + 2,6-dichlorophenolindophenol
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2-oxovalerate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-butanoyldihydrolipoyllysine + CO2
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2-oxovalerate is not a substrate for wild-type
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?
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
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thiamine diphosphate
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thiamine diphosphate
dependent
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Mg2+
1 mM used in assay conditions
Mg2+
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1 mM used in assay conditions
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0.11 - 11.1
2-oxo-5-hexenoic acid
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0.006 - 1.87
2-oxoglutarate
0.01 - 8.18
2-oxovalerate
0.11
2-oxo-5-hexenoic acid
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mutant E1o-H298D/E2o-S333M, pH not specified in the publication, temperature not specified in the publication
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0.5
2-oxo-5-hexenoic acid
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mutant E1o-H298D/E2o-H348F, pH not specified in the publication, temperature not specified in the publication
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0.73
2-oxo-5-hexenoic acid
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mutant E1o-H298D/E2o-H348Y, pH not specified in the publication, temperature not specified in the publication
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1.1
2-oxo-5-hexenoic acid
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mutant E1o-H298D/E2o-H348Q, pH not specified in the publication, temperature not specified in the publication
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8.01
2-oxo-5-hexenoic acid
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wild type enzyme, at pH 8.0 and 30°C
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11.1
2-oxo-5-hexenoic acid
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mutant enzyme H298D, at pH 8.0 and 30°C
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0.006
2-oxoglutarate
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wild type enzyme, at pH 8.0 and 30°C
0.02
2-oxoglutarate
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mutant E1o-H298D/E2o-H348Y, pH not specified in the publication, temperature not specified in the publication
0.03
2-oxoglutarate
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mutant E1o-H298D, pH not specified in the publication, temperature not specified in the publication
0.03
2-oxoglutarate
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mutant E1o-H298D/E2o-H348F, pH not specified in the publication, temperature not specified in the publication
0.04
2-oxoglutarate
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wild-type, pH not specified in the publication, temperature not specified in the publication
0.04
2-oxoglutarate
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mutant E1o-H298D/E2o-S333M, pH not specified in the publication, temperature not specified in the publication
0.07
2-oxoglutarate
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mutant E1o-H298D/E2o-H348Q, pH not specified in the publication, temperature not specified in the publication
1.87
2-oxoglutarate
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mutant enzyme H298D, at pH 8.0 and 30°C
0.01
2-oxovalerate
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mutant E1o-H298D/E2o-H348F, pH not specified in the publication, temperature not specified in the publication
0.01
2-oxovalerate
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mutant E1o-H298D/E2o-H348Y, pH not specified in the publication, temperature not specified in the publication
0.05
2-oxovalerate
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mutant E1o-H298D/E2o-H348Q, pH not specified in the publication, temperature not specified in the publication
0.08
2-oxovalerate
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mutant E1o-H298D/E2o-S333M, pH not specified in the publication, temperature not specified in the publication
6.62
2-oxovalerate
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mutant enzyme H298D, at pH 8.0 and 30°C
8.18
2-oxovalerate
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wild type enzyme, at pH 8.0 and 30°C
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0.0595 - 1.68
2-oxo-5-hexenoic acid
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0.152 - 0.81
2-oxovalerate
0.0595
2-oxo-5-hexenoic acid
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wild type enzyme, at pH 8.0 and 30°C
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0.148
2-oxo-5-hexenoic acid
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mutant enzyme H298D, at pH 8.0 and 30°C
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0.65
2-oxo-5-hexenoic acid
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mutant E1o-H298D/E2o-H348Q, pH not specified in the publication, temperature not specified in the publication
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0.86
2-oxo-5-hexenoic acid
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mutant E1o-H298D/E2o-H348Y, pH not specified in the publication, temperature not specified in the publication
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0.99
2-oxo-5-hexenoic acid
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mutant E1o-H298D/E2o-H348F, pH not specified in the publication, temperature not specified in the publication
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1.68
2-oxo-5-hexenoic acid
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mutant E1o-H298D/E2o-S333M, pH not specified in the publication, temperature not specified in the publication
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0.73
2-oxoglutarate
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mutant enzyme H298D, at pH 8.0 and 30°C
2.7
2-oxoglutarate
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wild type enzyme, at pH 8.0 and 30°C
6.8
2-oxoglutarate
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mutant E1o-H298D/E2o-H348Y, pH not specified in the publication, temperature not specified in the publication
7.3
2-oxoglutarate
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mutant E1o-H298D/E2o-H348F, pH not specified in the publication, temperature not specified in the publication
8.4
2-oxoglutarate
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mutant E1o-H298D/E2o-S333M, pH not specified in the publication, temperature not specified in the publication
10.5
2-oxoglutarate
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mutant E1o-H298D/E2o-H348Q, pH not specified in the publication, temperature not specified in the publication
21.1
2-oxoglutarate
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mutant E1o-H298D, pH not specified in the publication, temperature not specified in the publication
35
2-oxoglutarate
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wild-type, pH not specified in the publication, temperature not specified in the publication
0.152
2-oxovalerate
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wild type enzyme, at pH 8.0 and 30°C
0.34
2-oxovalerate
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mutant E1o-H298D/E2o-H348Q, pH not specified in the publication, temperature not specified in the publication
0.38
2-oxovalerate
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mutant E1o-H298D/E2o-S333M, pH not specified in the publication, temperature not specified in the publication
0.48
2-oxovalerate
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mutant enzyme H298D, at pH 8.0 and 30°C
0.57
2-oxovalerate
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mutant E1o-H298D/E2o-H348Y, pH not specified in the publication, temperature not specified in the publication
0.81
2-oxovalerate
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mutant E1o-H298D/E2o-H348F, pH not specified in the publication, temperature not specified in the publication
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0.0074 - 0.0134
2-oxo-5-hexenoate
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0.59 - 15.3
2-oxo-5-hexenoic acid
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0.39 - 875
2-oxoglutarate
0.0165 - 81
2-oxovalerate
0.0074
2-oxo-5-hexenoate
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wild type enzyme, at pH 8.0 and 30°C
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0.0134
2-oxo-5-hexenoate
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mutant enzyme H298D, at pH 8.0 and 30°C
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0.59
2-oxo-5-hexenoic acid
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mutant E1o-H298D/E2o-H348Q, pH not specified in the publication, temperature not specified in the publication
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1.17
2-oxo-5-hexenoic acid
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mutant E1o-H298D/E2o-H348Y, pH not specified in the publication, temperature not specified in the publication
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1.98
2-oxo-5-hexenoic acid
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mutant E1o-H298D/E2o-H348F, pH not specified in the publication, temperature not specified in the publication
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15.3
2-oxo-5-hexenoic acid
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mutant E1o-H298D/E2o-S333M, pH not specified in the publication, temperature not specified in the publication
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0.39
2-oxoglutarate
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mutant enzyme H298D, at pH 8.0 and 30°C
149
2-oxoglutarate
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mutant E1o-H298D/E2o-H348Q, pH not specified in the publication, temperature not specified in the publication
210
2-oxoglutarate
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mutant E1o-H298D/E2o-S333M, pH not specified in the publication, temperature not specified in the publication
244
2-oxoglutarate
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mutant E1o-H298D/E2o-H348F, pH not specified in the publication, temperature not specified in the publication
338
2-oxoglutarate
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mutant E1o-H298D/E2o-H348Y, pH not specified in the publication, temperature not specified in the publication
456.6
2-oxoglutarate
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wild type enzyme, at pH 8.0 and 30°C
703
2-oxoglutarate
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mutant E1o-H298D, pH not specified in the publication, temperature not specified in the publication
875
2-oxoglutarate
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wild-type, pH not specified in the publication, temperature not specified in the publication
0.0165
2-oxovalerate
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wild type enzyme, at pH 8.0 and 30°C
0.0725
2-oxovalerate
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mutant enzyme H298D, at pH 8.0 and 30°C
4.7
2-oxovalerate
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mutant E1o-H298D/E2o-S333M, pH not specified in the publication, temperature not specified in the publication
6.8
2-oxovalerate
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mutant E1o-H298D/E2o-H348Q, pH not specified in the publication, temperature not specified in the publication
57
2-oxovalerate
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mutant E1o-H298D/E2o-H348Y, pH not specified in the publication, temperature not specified in the publication
81
2-oxovalerate
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mutant E1o-H298D/E2o-H348F, pH not specified in the publication, temperature not specified in the publication
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0.0168
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wild type enzyme, with 2-oxo-5-hexenoate as substrate, at pH 8.0 and 30°C
0.042
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mutant enzyme H298D, with 2-oxo-5-hexenoate as substrate, at pH 8.0 and 30°C
0.0429
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wild type enzyme, with 2-oxovalerate as substrate, at pH 8.0 and 30°C
0.135
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mutant enzyme H298D, with 2-oxovalerate as substrate, at pH 8.0 and 30°C
0.206
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mutant enzyme H298D, with 2-oxoglutarate as substrate, at pH 8.0 and 30°C
0.775
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wild type enzyme, with 2-oxoglutarate as substrate, at pH 8.0 and 30°C
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Uniprot
brenda
i.e. SucA, subunit E1 of the 2-oxoglutarate dehydrogenase complex
Uniprot
brenda
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210000
2 * 105000, SDS-PAGE
104805
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x * 104805, 2-oxoglutarate dehydrogenase subunit, calculation from nucleotide sequence
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homodimer
x-ray crystallography
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x * 104805, 2-oxoglutarate dehydrogenase subunit, calculation from nucleotide sequence
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x * 105000, calculated from amino acid sequence
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sitting drop vapour diffusion method with 12% (w/v) polyethylene glycol 4000, 50 mM sodium citrate (pH 5.6)
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H260A
mutant has a dramatically reduced catalytic rate
H298A
mutant has a dramatically reduced catalytic rate
H348F
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mutation in subunit Eo, leads to activity for 2-oxovalerate in the reconstituted complex with E1o-H298D
H348Q
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mutation in subunit Eo, leads to activity for 2-oxovalerate in the reconstituted complex with E1o-H298D
H348Y
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mutation in subunit Eo, leads to activity for 2-oxovalerate in the reconstituted complex with E1o-H298D
S333M
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mutation in subunit Eo, leads to activity for 2-oxovalerate in the reconstituted complex with E1o-H298D
additional information
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conversion of enzyme from a 2-oxoglutarate dehydrogenase to a 2-oxo aliphatic dehydrogenase complex by evolving the E1o and E2o components. Mutants E2o-S333M, E2o-H348F, E2o-H348Q, and E2o-H348Y show activity for 2-oxovalerate in the reconstituted complex with E1o-H298D
H298D
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mutation in subunit E1o, active for 2-oxovalerate in an E1o-specific assay
H298D
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the mutant enzyme shows 4.4fold increased activity toward 2-oxovalerate and 1200fold decreased activity toward 2-oxoglutarate compared to the wild type enzyme
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ammonium sulfate precipitation, HiLoad Q-Sepharose column chromatography, and Superdex S200 gel filtration
Sephacryl S-500 gel filtration
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expressed in Escherichia coli BL21(DE3) cells
expressed in Saccharomyces cerevisiae cytosol
expressed in Escherichia coli JW0715 cells
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synthesis
expression of the structural genes for all three subunits of the Escherichia coli 2-oxoglutarate dehydrogenase complex in Saccharomyces cerevisiae. The Escherichia coli lipoic-acid scavenging enzyme is coexpressed to enable cytosolic lipoylation of the complex, which is required for its enzymatic activity. In vivo cytosolic activity of the complex is tested by constructing a reporter strain in which the essential metabolite 5-aminolevulinic acid can only be synthetized from cytosolic, and not mitochondrial, succinyl-CoA. In the resulting strain, complementation of 5-aminolevulinic acid auxotrophy depends on activation of the 2-oxoglutarate dehydrogenase complex by lipoic acid addition
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Guest, J.R.; Darlison, M.G.; Spencer, M.E.; Stephens, P.E.
Cloning and sequence analysis of the pyruvate and 2-oxoglutarate dehydrogenase complex genes of Escherichia coli
Biochem. Soc. Trans.
12
220-223
1984
Escherichia coli
brenda
Jones, D.D.; Perham, R.N.
The role of loop and beta-turn residues as structural and functional determinants for the lipoyl domain from the Escherichia coli 2-oxoglutarate dehydrogenase complex
Biochem. J.
409
357-366
2008
Escherichia coli
brenda
Frank, R.A.; Price, A.J.; Northrop, F.D.; Perham, R.N.; Luisi, B.F.
Crystal structure of the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex
J. Mol. Biol.
368
639-651
2007
Escherichia coli (P0AFG3), Escherichia coli
brenda
Chakraborty, J.; Nemeria, N.; Zhang, X.; Nareddy, P.; Szostak, M.; Farinas, E.; Jordan, F.
Engineering 2-oxoglutarate dehydrogenase to a 2-oxo aliphatic dehydrogenase complex by optimizing consecutive components
AIChE J.
66
e16769
2020
Escherichia coli
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brenda
Baldi, N.; Dykstra, J.C.; Luttik, M.A.H.; Pabst, M.; Wu, L.; Benjamin, K.R.; Vente, A.; Pronk, J.T.; Mans, R.
Functional expression of a bacterial alpha-ketoglutarate dehydrogenase in the cytosol of Saccharomyces cerevisiae
Metab. Eng.
56
190-197
2019
Escherichia coli (P0AFG3)
brenda