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Information on EC 1.2.4.2 - oxoglutarate dehydrogenase (succinyl-transferring) and Organism(s) Escherichia coli and UniProt Accession P0AFG3

for references in articles please use BRENDA:EC1.2.4.2
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IUBMB Comments
Contains thiamine diphosphate. It is a component of the multienzyme 2-oxoglutarate dehydrogenase complex 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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This record set is specific for:
Escherichia coli
UNIPROT: P0AFG3
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The taxonomic range for the selected organisms is: Escherichia coli
Synonyms
2-ketoglutarate dehydrogenase, 2-OGDH, 2-oxoglutarate decarboxylase, 2-oxoglutarate dehydrogenase, 2-oxoglutarate dehydrogenase complex, 2-oxoglutarate dehydrogenase complex E1 component, 2-oxoglutarate dehydrogenase-like protein, 2-oxoglutarate:lipoate oxidoreductase, 2OGDH, AKGDH, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-ketoglutarate dehydrogenase
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2-OGDH
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2-oxoglutarate decarboxylase
2-oxoglutarate dehydrogenase
2-oxoglutarate:lipoate oxidoreductase
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-
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2OGDH
246
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AKGDH
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alpha-ketoglutarate dehydrogenase
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-
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alpha-ketoglutarate dehydrogenase complex
246
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alpha-ketoglutaric acid dehydrogenase
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alpha-ketoglutaric dehydrogenase
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alpha-KGD
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alpha-oxoglutarate dehydrogenase
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dehydrogenase, oxoglutarate
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E1 component of the 2-oxoglutarate dehydrogenase multienzyme complex
246
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E1o component
246
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E2
246
component of the 2-oxo acid dehydrogenase multienzyme complex
ketoglutaric dehydrogenase
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OGDC
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oxoglutarate decarboxylase
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oxoglutarate dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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oxidative decarboxylation
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redox reaction
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reduction
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SYSTEMATIC NAME
IUBMB Comments
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 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.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-02-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
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-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
show the reaction diagram
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ir
additional information
?
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substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
dependent
additional information
-
lipoyl moiety, LipS2, is bound in amide linkage to the epsilon amino group of a lysine residue
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
Ca2+ is no activator
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-oxo-3-carboxypropylphosphonic acid methyl ester
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glyoxylate
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2-oxoglutarate dehydrogenase complex
succinyl phosphonate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
2-oxoglutarate
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-
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.7
glyoxylate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
specific activity of the 2-oxoglutarate dehydrogenase complex
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Uniprot
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
104805
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x * 104805, 2-oxoglutarate dehydrogenase subunit, calculation from nucleotide sequence
190000
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2-oxoglutarate dehydrogenase component, equilibrium sedimentation
210000
2 * 105000, SDS-PAGE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 104805, 2-oxoglutarate dehydrogenase subunit, calculation from nucleotide sequence
homodimer
x-ray crystallography
additional information
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion method with 12% (w/v) polyethylene glycol 4000, 50 mM sodium citrate (pH 5.6)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H260A
mutant has a dramatically reduced catalytic rate
H298A
mutant has a dramatically reduced catalytic rate
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
2-oxoglutarate dehydrogenase complex
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ammonium sulfate precipitation, HiLoad Q-Sepharose column chromatography, and Superdex S200 gel filtration
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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alpha-ketoglutarate-involving reactions belong to the backbone of high-flux reactions, which is rather conserved in evolution
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Reed, L.J.; Cox, D.J.
Multienzyme complexes
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
1
213-240
1970
Bos taurus, Escherichia coli, Sus scrofa
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Reed, L.J.; Mukherjee, B.B.
alpha-Ketoglutarate dehydrogenase complex from Escherichia coli
Methods Enzymol.
13
55-61
1969
Escherichia coli
-
Manually annotated by BRENDA team
Gupta, S.C.; Dekker, E.E.
Evidence for the identity and some comparative properties of alpha-ketoglutarate and 2-keto-4-hydroxyglutarate dehydrogenase activity
J. Biol. Chem.
255
1107-1112
1980
Escherichia coli, Sus scrofa
Manually annotated by BRENDA team
Gupta, S.C.; Dekker, E.E.
Oxidation of 2-keto-4-hydroxyglutarate by pig heart and Escherichia coli alpha-ketoglutarate dehydrogenase complex
Arch. Biochem. Biophys.
192
324-326
1979
Escherichia coli, Sus scrofa
Manually annotated by BRENDA team
Waskiewicz, D.E.; Hammes, G.G.
Elementary steps in the reaction mechanism of the alpha-ketoglutarate dehydrogenase multienzyme complex from Escherichia coli: kinetics of succinylation and desuccinylation
Biochemistry
23
3136-3143
1984
Escherichia coli
Manually annotated by BRENDA team
Pettit, F.H.; Hamilton, L.; Munk, P.; Namihira, G.; Eley, M.H.; Willms, C.R.; Reed, L.J.
alpha-Keto acid dehydrogenase complexes. XIX. Subunit structure of the Escherichia coli alpha-ketoglutarate dehydrogenase complex
J. Biol. Chem.
248
5282-5290
1973
Escherichia coli
Manually annotated by BRENDA team
Biryukov, A.I.; Bunik, V.I.; Zhukov, Y.N.; Khurs, E.N.; Khomutov, R.M.
Succinyl phosphonate inhibits alpha-ketoglutarate oxidative decarboxylation, catalyzed by alpha-ketoglutarate dehydrogenase complexes from E. coli and pigeon breast muscle
FEBS Lett.
382
167-170
1996
Escherichia coli, Pigeon
Manually annotated by BRENDA team
Perham, R.N.; Jones, D.D.; Chauhan, H.J.; Howard, M.J.
Substrate channeling in 2-oxo acid dehydrogenase multienzyme complexes
Biochem. Soc. Trans.
30
47-51
2002
Azotobacter vinelandii, Escherichia coli, Geobacillus stearothermophilus, Pseudomonas putida
Manually annotated by BRENDA team
Strumilo, S.
Short-term regulation of the alpha-ketoglutarate dehydrogenase complex by energy-linked and some other effectors
Biochemistry
70
726-729
2005
Bison bison, Bos taurus, Columba livia, Escherichia coli, Homo sapiens, Rattus norvegicus, Solanum tuberosum, Sus scrofa
Manually annotated by BRENDA team
Gibson, G.E.; Blass, J.P.; Beal, M.F.; Bunik, V.
The alpha-ketoglutarate-dehydrogenase complex: a mediator between mitochondria and oxidative stress in neurodegeneration
Mol. Neurobiol.
31
43-63
2005
Bos taurus, Escherichia coli, Homo sapiens, Mesocricetus auratus, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Sus scrofa
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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, Escherichia coli (P0AFG3)
Manually annotated by BRENDA team
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