Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-ketoglutarate dehydrogenase
2-oxoglutarate decarboxylase
2-oxoglutarate dehydrogenase
2-oxoglutarate dehydrogenase complex
2-oxoglutarate dehydrogenase complex E1 component
-
-
2-oxoglutarate dehydrogenase-like protein
-
brain-specific isozyme
2-oxoglutarate:lipoate oxidoreductase
-
-
-
-
alpha-ketoglutarate dehydrogenase
alpha-ketoglutarate dehydrogenase multienzyme complex
alpha-ketoglutaric acid dehydrogenase
-
-
-
-
alpha-ketoglutaric dehydrogenase
-
-
-
-
alpha-oxoglutarate dehydrogenase
-
-
-
-
dehydrogenase, oxoglutarate
-
-
-
-
E1 component of the 2-oxoglutarate dehydrogenase multienzyme complex
-
E1 subunit of the alpha-ketoglutarate dehydrogenase complex
-
-
E1k
-
part of the alpha-ketoglutarate dehydrogenase complex
E1o component 2-oxoglutarate dehydrogenase complex
-
-
ketoglutaric dehydrogenase
-
-
-
-
OGDHL
-
brain-specific isozyme
oxoglutarate decarboxylase
-
-
-
-
oxoglutarate dehydrogenase
2-ketoglutarate dehydrogenase
-
-
-
-
2-ketoglutarate dehydrogenase
-
-
2-oxoglutarate decarboxylase
-
part of the 2-oxoglutarate dehydrogenase complex
2-oxoglutarate decarboxylase
-
2-oxoglutarate dehydrogenase
-
-
-
-
2-oxoglutarate dehydrogenase
-
-
2-oxoglutarate dehydrogenase
-
-
2-oxoglutarate dehydrogenase
-
-
2-oxoglutarate dehydrogenase
-
first and rate-limiting component of the multienzyme 2-oxoglutarate dehydrogenase complex
2-oxoglutarate dehydrogenase
-
2-oxoglutarate dehydrogenase
-
-
2-oxoglutarate dehydrogenase complex
-
-
2-oxoglutarate dehydrogenase complex
-
-
alpha-ketoglutarate dehydrogenase
-
-
-
-
alpha-ketoglutarate dehydrogenase
-
-
alpha-ketoglutarate dehydrogenase
-
-
alpha-ketoglutarate dehydrogenase
-
-
alpha-ketoglutarate dehydrogenase
-
-
alpha-ketoglutarate dehydrogenase multienzyme complex
-
-
alpha-ketoglutarate dehydrogenase multienzyme complex
-
-
alpha-KGDH
-
-
E1o
-
-
E1o
-
component of the alpha-ketoglutarate dehydrogenase multienzyme complex KGDH consisting of components E1o, EC 1.2.4.2, E2, EC 2.1.3.6, and E3, EC 1.8.1.4
E1o
component of the 2-oxoglutarate dehydrogenase multienzyme complex
KGDH
-
-
KGDHC
-
-
ODH
-
-
OdhA
-
-
OGDH
-
-
OGDH
-
part of the 2-oxoglutarate dehydrogenase complex multienzyme system
oxoglutarate dehydrogenase
-
-
-
-
oxoglutarate dehydrogenase
-
-
oxoglutarate dehydrogenase
-
-
-
oxoglutarate dehydrogenase
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)
-
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)
-
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)
-
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)
-
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)
-
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)
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-oxoglutarate + CoA
? + H2O2
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
additional information
?
-
2-oxoglutarate + CoA
? + H2O2
-
-
-
-
?
2-oxoglutarate + CoA
? + H2O2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
transcription of the 2-oxoglutarate dehydrogenase component of the 2-oxoglutarate dehydrogenase complex is regulated by glucose and activated by the products of HAP2 and HAP3
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
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 + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
?
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 + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
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 + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
additional information
?
-
-
enzyme also catalyzes the production of H2O2 in vivo, in vitro, and in situ from 2-oxoglutarate with CoA in absence of NAD+, which inhibits this reaction, enzyme is a atrget for reactive oxygen species and also contributes to generation of oxidative stress in mitochondria when NADH oxidation is impaired, overview
-
-
?
additional information
?
-
-
OdhA can utilize free dihydrodilipoamide to perform the E2 reaction specifically with succinyl-CoA. OdhA specifically catalyzes the E1 and E2 reaction to convert 2-oxoglutarate to succinyl-CoA but fully relies on the lipoyl residues provided by AceF involved in the reactions to convert pyruvate to acetyl-CoA
-
-
?
additional information
?
-
-
OdhA can utilize free dihydrodilipoamide to perform the E2 reaction specifically with succinyl-CoA. OdhA specifically catalyzes the E1 and E2 reaction to convert 2-oxoglutarate to succinyl-CoA but fully relies on the lipoyl residues provided by AceF involved in the reactions to convert pyruvate to acetyl-CoA
-
-
?
additional information
?
-
-
enzyme complex produces H2O2 in vivo, which is inhibited by NAD+ with the isolated enzyme complex and in mitochondria, physiological effects and regulation, overview
-
-
?
additional information
?
-
-
enzyme complex produces H2O2 in vivo, which is inhibited by NAD+ with the isolated enzyme complex and in mitochondria, physiological effects and regulation, overview
-
-
?
additional information
?
-
-
the E1o component of the2-oxoglutarate dehydrogenase complex catalyses the initial, substrate-specific and irreversible stage of the overall reaction, and has the lowest catalytic activity (turnover number) among the components and as such limits the rate of the overall process
-
-
?
additional information
?
-
-
enzyme also catalyzes the production of H2O2 from 2-oxoglutarate with CoA in absence of NAD+, which inhibits this reaction, enzyme is a target for reactive oxygen species and also contributes to generation of oxidative stress in mitochondria when NADH oxidation is impaired, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
transcription of the 2-oxoglutarate dehydrogenase component of the 2-oxoglutarate dehydrogenase complex is regulated by glucose and activated by the products of HAP2 and HAP3
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
additional information
?
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
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 + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
additional information
?
-
-
enzyme also catalyzes the production of H2O2 in vivo, in vitro, and in situ from 2-oxoglutarate with CoA in absence of NAD+, which inhibits this reaction, enzyme is a atrget for reactive oxygen species and also contributes to generation of oxidative stress in mitochondria when NADH oxidation is impaired, overview
-
-
?
additional information
?
-
-
OdhA can utilize free dihydrodilipoamide to perform the E2 reaction specifically with succinyl-CoA. OdhA specifically catalyzes the E1 and E2 reaction to convert 2-oxoglutarate to succinyl-CoA but fully relies on the lipoyl residues provided by AceF involved in the reactions to convert pyruvate to acetyl-CoA
-
-
?
additional information
?
-
-
OdhA can utilize free dihydrodilipoamide to perform the E2 reaction specifically with succinyl-CoA. OdhA specifically catalyzes the E1 and E2 reaction to convert 2-oxoglutarate to succinyl-CoA but fully relies on the lipoyl residues provided by AceF involved in the reactions to convert pyruvate to acetyl-CoA
-
-
?
additional information
?
-
-
enzyme complex produces H2O2 in vivo, which is inhibited by NAD+ with the isolated enzyme complex and in mitochondria, physiological effects and regulation, overview
-
-
?
additional information
?
-
-
enzyme complex produces H2O2 in vivo, which is inhibited by NAD+ with the isolated enzyme complex and in mitochondria, physiological effects and regulation, overview
-
-
?
additional information
?
-
-
the E1o component of the2-oxoglutarate dehydrogenase complex catalyses the initial, substrate-specific and irreversible stage of the overall reaction, and has the lowest catalytic activity (turnover number) among the components and as such limits the rate of the overall process
-
-
?
additional information
?
-
-
enzyme also catalyzes the production of H2O2 from 2-oxoglutarate with CoA in absence of NAD+, which inhibits this reaction, enzyme is a target for reactive oxygen species and also contributes to generation of oxidative stress in mitochondria when NADH oxidation is impaired, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Schulze, E.; Westphal, A.H.; Hanemaaijer, R.; de Kok A.
The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 1. Molecular cloning and sequence analysis of the gene encoding the 2-oxoglutarate dehydrogenase component
Eur. J. Biochem.
187
229-234
1990
Azotobacter vinelandii
brenda
Carlsson, P.; Hederstedt, L.
Genetic characterization of Bacillus subtilis odhA and odhB, encoding 2-oxoglutarate dehydrogenase and dihydrolipoamide transsuccinylase, respectively
J. Bacteriol.
171
3667-3672
1989
Bacillus subtilis
brenda
Repetto, B.; Tzagoloff, A.
Structure and regulation of KGD1, the structural gene for yeast alpha-ketoglutarate dehydrogenase
Mol. Cell. Biol.
9
2695-2705
1989
Saccharomyces cerevisiae
brenda
Karam, G.A.; Bishop, S.H.
alpha-Ketoglutarate dehydrogenase from cauliflower mitochondria: preparation and reactivity with substrates
Phytochemistry
28
3291-3293
1989
Brassica oleracea
-
brenda
Dry, I.B.; Wiskich, J.T.
2-Oxoglutarate dehydrogenase and pyruvate dehydrogenase activities in plant mitochondria: interaction via a common coenzyme a pool
Arch. Biochem. Biophys.
257
92-99
1987
Brassica rapa, Pisum sativum
brenda
Burke, L.A.; Heffron, J.J.A.
Isocitrate and oxoglutarate dehydrogenase activities of murine dystrophic skeletal muscle
Biochem. Soc. Trans.
15
233-234
1987
Mus musculus
-
brenda
De Marcucci, O.G.L.; Hunter, A.; Lindsay, J.G.
Precursor forms of the constituent polypeptides of pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes from ox heart
Biochem. Soc. Trans.
14
870
1986
Bos taurus
-
brenda
Hunter, A.; Lindsay, J.G.
Immunological and biosynthetic studies on the mammalian 2-oxoglutarate dehydrogenase multienzyme complex
Eur. J. Biochem.
155
103-109
1986
Bos taurus
brenda
Hein, S.; Steinbuechel, A.
Cloning and characterization of the Alcaligenes eutrophus 2-oxoglutarate dehydrogenase complex
FEMS Microbiol. Lett.
136
231-238
1996
Cupriavidus necator
brenda
Nichols, B.J.; Rigoulet, M.; Denton, R.M.
Comparison of the effects of Ca2+, adenine nucleotides and pH on the kinetic properties of mitochondrial NAD+-isocitrate dehydrogenase and oxoglutarate dehydrogenase from the yeast Saccharomyces cerevisiae and rat heart
Biochem. J.
303
461-465
1994
Rattus norvegicus, Saccharomyces cerevisiae
brenda
Nulton-Persson, A.C.; Starke, D.W.; Mieyal, J.J.; Szweda, L.I.
Reversible inactivation of alpha-ketoglutarate dehydrogenase in response to alterations in the mitochondrial glutathione status
Biochemistry
42
4235-4242
2003
Rattus norvegicus
brenda
Kim, C.H.
Catalytic domain of Salmonella typhimurium 2-oxoglutarate dehydrogenase is localized in N-terminal region
J. Mol. Catal. B
26
193-200
2003
Salmonella enterica subsp. enterica serovar Typhimurium (O87668)
-
brenda
Tretter, L.; Adam-Vizi, V.
Generation of reactive oxygen species in the reaction catalyzed by alpha-ketoglutarate dehydrogenase
J. Neurosci.
24
7771-7778
2004
Cavia porcellus, Sus scrofa
brenda
Starkov, A.A.; Fiskum, G.; Chinopoulos, C.; Lorenzo, B.J.; Browne, S.E.; Patel, M.S.; Beal, M.F.
Mitochondrial alpha-ketoglutarate dehydrogenase complex generates reactive oxygen species
J. Neurosci.
24
7779-7788
2004
Mus musculus, Rattus norvegicus
brenda
McMillan, P.J.; Stimmler, L.M.; Foth, B.J.; McFadden, G.I.; Mueller, S.
The human malaria parasite Plasmodium falciparum possesses two distinct dihydrolipoamide dehydrogenases
Mol. Microbiol.
55
27-38
2005
Plasmodium falciparum
brenda
Solien, J.; Haynes, V.; Giulivi, C.
Differential requirements of calcium for oxoglutarate dehydrogenase and mitochondrial nitric-oxide synthase under hypoxia: Impact on the regulation of mitochondrial oxygen consumption
Comp. Biochem. Physiol. A
142A
111-117
2005
Rattus norvegicus
-
brenda
Niebisch, A.; Kabus, A.; Schultz, C.; Weil, B.; Bott, M.
Corynebacterial protein kinase G controls 2-oxoglutarate dehydrogenase activity via the phosphorylation status of the OdhI protein
J. Biol. Chem.
281
12300-12307
2006
Corynebacterium glutamicum
brenda
Tian, J.; Bryk, R.; Shi, S.; Erdjument-Bromage, H.; Tempst, P.; Nathan, C.
Mycobacterium tuberculosis appears to lack alpha-ketoglutarate dehydrogenase and encodes pyruvate dehydrogenase in widely separated genes
Mol. Microbiol.
57
859-868
2005
no activity in Mycobacterium tuberculosis
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
Shi, Q.; Karuppagounder, S.S.; Xu, H.; Pechman, D.; Chen, H.; Gibson, G.E.
Responses of the mitochondrial alpha-ketoglutarate dehydrogenase complex to thiamine deficiency may contribute to regional selective vulnerability
Neurochem. Int.
50
921-931
2007
Mus musculus
brenda
Bunik, V.I.; Fernie, A.R.
Metabolic control exerted by the 2-oxoglutarate dehydrogenase reaction: a cross-kingdom comparison of the crossroad between energy production and nitrogen assimilation
Biochem. J.
422
405-421
2009
Rattus norvegicus
brenda
Bunik, V.; Kaehne, T.; Degtyarev, D.; Shcherbakova, T.; Reiser, G.
Novel isoenzyme of 2-oxoglutarate dehydrogenase is identified in brain, but not in heart
FEBS J.
275
4990-5006
2008
Rattus norvegicus
brenda
Mailloux, R.J.; Singh, R.; Brewer, G.; Auger, C.; Lemire, J.; Appanna, V.D.
alpha-Ketoglutarate dehydrogenase and glutamate dehydrogenase work in tandem to modulate the antioxidant alpha-ketoglutarate during oxidative stress in Pseudomonas fluorescens
J. Bacteriol.
191
3804-3810
2009
Pseudomonas fluorescens
brenda
Graf, A.; Kabysheva, M.; Klimuk, E.; Trofimova, L.; Dunaeva, T.; ZÃ1/4ndorf, G.; Kahlert, S.; Reiser, G.; Storozhevykh, T.; Pinelis, V.; Sokolova, N.; Bunik, V.
Role of 2-oxoglutarate dehydrogenase in brain pathologies involving glutamate neurotoxicity
J. Mol. Catal. B
61
80-87
2009
Rattus norvegicus
-
brenda
Ambrus, A.; Tretter, L.; Adam-Vizi, V.
Inhibition of the alpha-ketoglutarate dehydrogenase-mediated reactive oxygen species generation by lipoic acid
J. Neurochem.
109 Suppl 1
222-229
2009
Cavia porcellus
brenda
Hoffelder, M.; Raasch, K.; van Ooyen, J.; Eggeling, L.
The E2 domain of OdhA of Corynebacterium glutamicum has succinyltransferase activity dependent on lipoyl residues of the acetyltransferase AceF
J. Bacteriol.
192
5203-5211
2010
Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032
brenda
Mailloux, R.J.; Gardiner, D.; OBrien, M.
2-Oxoglutarate dehydrogenase is a more significant source of O2(-)/H2O2 than pyruvate dehydrogenase in cardiac and liver tissue
Free Radic. Biol. Med.
97
501-512
2016
Sus scrofa
brenda
Zakharchenko, M.; Zakharchenko, A.; Khunderyakova, N.; Tutukina, M.; Simonova, M.; Vasilieva, A.; Romanova, O.; Fedotcheva, N.; Litvinova, E.; Maevsky, E.; Zinchenko, V.; Berezhnov, A.; Morgunov, I.; Gulayev, A.; Kondrashova, M.
Burst of succinate dehydrogenase and alpha-ketoglutarate dehydrogenase activity in concert with the expression of genes coding for respiratory chain proteins underlies short-term beneficial physiological stress in mitochondria
Int. J. Biochem. Cell Biol.
45
190-200
2013
Rattus norvegicus
brenda
Nemeria, N.S.; Ambrus, A.; Patel, H.; Gerfen, G.; Adam-Vizi, V.; Tretter, L.; Zhou, J.; Wang, J.; Jordan, F.
Human 2-oxoglutarate dehydrogenase complex E1 component forms a thiamin-derived radical by aerobic oxidation of the enamine intermediate
J. Biol. Chem.
289
29859-29873
2014
Homo sapiens
brenda
BRENDA home
History
1.2.4.2 oxoglutarate dehydrogenase (succinyl-transferring)
more
top
