1.2.1.105: 2-oxoglutarate dehydrogenase system

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For detailed information about 2-oxoglutarate dehydrogenase system, go to the full flat file.

Reaction

Synonyms

2-OGDH2, 2-oxoglutarate dehydrogenase, 2-oxoglutarate dehydrogenase complex, alpha-KDE2, alpha-ketoglutarate dehydrogenase, alpha-ketoglutarate dehydrogenase complex, alpha-KGDH, At3g55410, At5g65750, DHTKD1, dihydrolipoyl succinyltransferase E2, E1a, E1k, E1o, E2, KGDH, KGDHC, More, MPA24.10, ODGH, ODGH1, ODGH2, ODH, OGDC, OGDH, OGDHC, OGDHL, OGHDC-E2, PDHC, SucA, SucB

ECTree

     1 Oxidoreductases

         1.2 Acting on the aldehyde or oxo group of donors

             1.2.1 With NAD⁺ or NADP⁺ as acceptor

                1.2.1.105 2-oxoglutarate dehydrogenase system

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Results	in table
36	Activating Compound
7	AA Sequence
15	Application
7	Cloned(Commentary)
56	Cofactor
3	Crystallization (Commentary)
17	General Information
4	General Stability
5	IC50 Value
133	Inhibitors
19	kcat/KM [mM/s]
13	Ki Value [mM]
84	KM Value [mM]
53	Localization
30	Metals/Ions
14	Molecular Weight [Da]
31	Natural Substrates/ Products (Substrates)
132	Organism
9	Pathway
19	pH Optimum
6	pH Range
2	Posttranslational Modification
17	Protein Variants
18	Purification (Commentary)
69	Reaction
127	Reference
1	Renatured (Commentary)
110	Source Tissue
16	Specific Activity [micromol/min/mg]
1	Storage Stability
124	Substrates and Products (Substrate)
18	Subunits
143	Synonyms
1	Systematic Name
6	Temperature Optimum [°C]
1	Temperature Range [°C]
3	Temperature Stability [°C]
17	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.2.1.105 - 2-oxoglutarate dehydrogenase system

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

electron cryotomography, shows that the E1 and E3 subunits of the complex are flexibly tethered about 11 nm away from the E2 core

Escherichia coli

-

760205

solution structure of a 51-residue synthetic peptide comprising the dihydrolipoamide dehydrogenase (E3)-binding domain of the dihydrolipoamide succinyltransferase (E2) core of the 2-oxoglutarate dehydrogenase multienzyme complex

Escherichia coli

P0AFG6

758773

structure of the component E2 catalytic domain, to 3.0 A resolution using molecular replacement. The active site is located in the middle of a channel formed at the interface between two 3fold related subunits. Active-site residues are His375 and Thr323 and Asp379. Binding of the substrates to E2 catalytic domain is proposed to induce a change in the conformation of Asp379, allowing this residue to form a salt bridge with Arg 184. Residues Ser330, Ser333, and His348 form the succinyl-binding pocket

Escherichia coli

P0AFG6

759623