Literature summary for 1.2.4.2 extracted from

Niebisch, A.; Kabus, A.; Schultz, C.; Weil, B.; Bott, M.
Corynebacterial protein kinase G controls 2-oxoglutarate dehydrogenase activity via the phosphorylation status of the OdhI protein (2006), J. Biol. Chem., 281, 12300-12307.

Search for more literature for 1.2.4.2

Application

Application	Comment	Organism
industry	ODH is essential for glutamine utilization, regulatory mechanisms of reduced ODH activity that is essential for the industrial production of 1.5 million tons per year of glutamate with Corynebacterium glutamicum	Corynebacterium glutamicum

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli DH5alpha	Corynebacterium glutamicum

Protein Variants

Protein Variants	Comment	Organism
additional information	mutant deltapknG has a defect in glutamine utilization, which is abolished by additional deletion of odhI, mutant deltaodhI transformed with plasmid OdhI-T14A has a defect in glutamine utilization	Corynebacterium glutamicum

Inhibitors

Inhibitors	Comment	Organism	Structure
OdhI	unphosphorylated OdhI strongly inhibits ODH activity	Corynebacterium glutamicum

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
140000	-	OdhA, the E1 subunit of ODH	Corynebacterium glutamicum

Organism

Organism	UniProt	Comment	Textmining
Corynebacterium glutamicum	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
by affinity chromatography, purification of OdhI-T14A leads to specific copurification of OdhA, the E1 subunit of ODH	Corynebacterium glutamicum

Synonyms

Synonyms	Comment	Organism
2-oxoglutarate dehydrogenase	-	Corynebacterium glutamicum
2-oxoglutarate dehydrogenase complex	-	Corynebacterium glutamicum
ODH	-	Corynebacterium glutamicum

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.0000024	-	OdhI	unphosphorylated state	Corynebacterium glutamicum

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Release 2023.1 (January 2023)