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Literature summary for 1.2.4.2 extracted from

  • 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 (2010), J. Bacteriol., 192, 5203-5211.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
AceF acetyltransferase AceF Corynebacterium glutamicum

Protein Variants

Protein Variants Comment Organism
H352C the activity of the mutant is significantly reduced Corynebacterium glutamicum
H352C/Q356D the mutations fully prevent succinyltransferase activity Corynebacterium glutamicum
Q356D the activity of the mutant is slightly reduced Corynebacterium glutamicum
T294A the mutant shows almost no activity Corynebacterium glutamicum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.13
-
2-oxoglutarate in 50 mM TES (pH 7.7), 10 mM MgCl2, 3 mM L-cysteine, 2 mM NAD+, 0.9 mM thiamine diphosphate, 0.05 mM chlorpromazine, and 1.5 mM 2-oxoglutarate, temperature not specified in the publication Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine Corynebacterium glutamicum
-
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine Corynebacterium glutamicum ATCC 13032
-
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
?
additional information Corynebacterium glutamicum 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 Corynebacterium glutamicum ATCC 13032 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 ?
-
?

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum
-
-
-
Corynebacterium glutamicum ATCC 13032
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography Corynebacterium glutamicum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
-
Corynebacterium glutamicum [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
-
Corynebacterium glutamicum ATCC 13032 [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
?
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 Corynebacterium glutamicum ?
-
?
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 Corynebacterium glutamicum ATCC 13032 ?
-
?

Synonyms

Synonyms Comment Organism
ODH
-
Corynebacterium glutamicum
OdhA
-
Corynebacterium glutamicum
oxoglutarate dehydrogenase
-
Corynebacterium glutamicum

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate dependent on Corynebacterium glutamicum