Literature summary for 1.2.1.105 extracted from

Millar, A.H.; Hill, S.A.; Leaver, C.J.
Plant mitochondrial 2-oxoglutarate dehydrogenase complex purification and characterization in potato (1999), Biochem. J., 343 Pt 2, 327-334 .

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	-	Solanum tuberosum	5739	-

Organism

Organism	UniProt	Comment	Textmining
Solanum tuberosum	P81895 and P81896 and P80503	P81895 i.e. 2-oxoglutarate dehydrogenase, cf. EC 1.2.4.2, P81896 i.e. dihydrolipoamide-residue succinyltransferase component, cf. EC 2.3.1.61, P80503 i.e. dihydrolipoyl dehydrogenase, cf. EC 1.8.14	-

Renatured (Commentary)

Renatured (Comment)	Organism
purification from either membrane or soluble matrix fractions results in the increasing dependence of the activity on the addition of dihydrolipoamide dehydrogenase E3	Solanum tuberosum

Source Tissue

Source Tissue	Comment	Organism	Textmining
tuber	-	Solanum tuberosum	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
4.6	-	presence of exogenously added dihydrolipoamide dehydrogenase E3, pH 7.5, 25°C	Solanum tuberosum

Subunits

Subunits	Comment	Organism
multimer	x * 48000, x * 50000, i.e. dihydrolipoamide succinyltransferases, x * 105000, i.e. 2-oxoglutarate dehydrogenase subunit, plus minor amounts of E3 polypeptides of 57000 and 58000 Da, SDS-PAGE	Solanum tuberosum

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Release 2023.1 (January 2023)