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Literature summary extracted from

  • Reed, L.J.; Cox, D.J.
    Multienzyme complexes (1970), The Enzymes, 3rd Ed. (Boyer, P. D. , ed. ), 1, 213-240.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.104 acetyl-CoA reversed by CoA Escherichia coli
1.2.1.104 additional information not inhibited by ATP Escherichia coli
1.2.1.104 phosphorylation
-
Bos taurus
1.2.1.104 phosphorylation
-
Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.104 additional information
-
-
Bos taurus
1.2.1.104 additional information
-
MW of native complex from heart: 740000 Da Sus scrofa
2.3.1.61 1000000
-
-
Escherichia coli
2.3.1.61 1000000
-
-
Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.61 succinyl-CoA + dihydrolipoamide Escherichia coli
-
CoA + S-succinyldihydrolipoamide
-
?
2.3.1.61 succinyl-CoA + dihydrolipoamide Sus scrofa
-
CoA + S-succinyldihydrolipoamide
-
?
2.3.1.61 succinyl-CoA + dihydrolipoamide Bos taurus
-
CoA + S-succinyldihydrolipoamide
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.104 Bos taurus
-
-
-
1.2.1.104 Escherichia coli
-
-
-
1.2.1.104 Sus scrofa
-
-
-
1.2.1.105 Bos taurus
-
-
-
1.2.1.105 Escherichia coli
-
-
-
1.2.1.105 Sus scrofa
-
-
-
2.3.1.61 Bos taurus
-
-
-
2.3.1.61 Escherichia coli
-
-
-
2.3.1.61 Sus scrofa
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.2.1.104 additional information not regulated by phosphorylation/dephosphorylation Escherichia coli
1.2.1.104 side-chain modification
-
Bos taurus
1.2.1.104 side-chain modification inactivated by phosphorylation 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 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) Escherichia coli
1.2.1.105 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) Sus scrofa
1.2.1.105 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) Bos taurus
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
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
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 Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.1.105 heart
-
Sus scrofa
-
1.2.1.105 heart
-
Bos taurus
-
1.2.1.105 kidney
-
Sus scrofa
-
1.2.1.105 kidney
-
Bos taurus
-
2.3.1.61 heart
-
Sus scrofa
-
2.3.1.61 kidney
-
Bos taurus
-

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 2-oxoglutarate + lipoamide
-
Bos taurus S-succinyldihydrolipoamide + CO2
-
?
2.3.1.61 succinyl-CoA + dihydrolipoamide
-
Escherichia coli CoA + S-succinyldihydrolipoamide
-
?
2.3.1.61 succinyl-CoA + dihydrolipoamide
-
Sus scrofa CoA + S-succinyldihydrolipoamide
-
?
2.3.1.61 succinyl-CoA + dihydrolipoamide
-
Bos taurus CoA + S-succinyldihydrolipoamide
-
?

Subunits

EC Number Subunits Comment Organism
2.3.1.61 polymer consists of 8 morphological subunits arranged in a cube-like structure Escherichia coli