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Information on EC 1.2.4.2 - oxoglutarate dehydrogenase (succinyl-transferring) and Organism(s) Bos taurus

for references in articles please use BRENDA:EC1.2.4.2
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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.
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Bos taurus
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Word Map
The taxonomic range for the selected organisms is: Bos taurus
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-ketoglutarate dehydrogenase
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2-OGDH
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2-oxoglutarate dehydrogenase
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-
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2-oxoglutarate:lipoate oxidoreductase
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AKGDH
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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-KGD
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alpha-oxoglutarate dehydrogenase
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dehydrogenase, oxoglutarate
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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, 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.
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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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
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required , 2-oxoglutarate dehydrogenase complex
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ODO1_BOVIN
1023
0
115808
Swiss-Prot
Mitochondrion (Reliability: 2)
A0A3Q1MVL5_BOVIN
1034
0
117117
TrEMBL
Mitochondrion (Reliability: 2)
A0A3Q1NKS6_BOVIN
1038
0
117538
TrEMBL
Mitochondrion (Reliability: 2)
F1MWG1_BOVIN
1010
0
114455
TrEMBL
Mitochondrion (Reliability: 1)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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Manually annotated by BRENDA team
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
Manually annotated by BRENDA team