Literature summary for 1.8.1.4 extracted from

Babady, N.E.; Pang, Y.P.; Elpeleg, O.; Isaya, G.
Cryptic proteolytic activity of dihydrolipoamide dehydrogenase (2007), Proc. Natl. Acad. Sci. USA, 104, 6158-6163.

Search for more literature for 1.8.1.4

Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	activation of DLD proteolytic activity by high salt concentrations during hydroxyapatite fractionation, Freezingthawing results in further activation	Sus scrofa
additional information	activation of DLD proteolytic activity by high salt concentrations during hydroxyapatite fractionation. Freezing-thawing results in further activation	Mus musculus

Application

Application	Comment	Organism
degradation	S456 and E431 form a catalytic dyad in the DLD monomer, whereas H450, by forming a hydrogen bond with E431, may decrease the ability of E431 to polarize the hydroxyl group of S456	Homo sapiens

Cloned(Commentary)

Cloned (Comment)	Organism
wild-type DLD and mutant D444V expressed in Escherichia coli BL21 with an N-terminal six-histidine tag. C-term DLD, the interface domain residing the proteolytic activity of DLD, expressed in Escherichia coli without any tags	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
D444V	shows weak proteolytic activity with mature frataxin substrate, but consistently cleaves mature frataxin to denoted frataxin products with faster kinetics than the wild-type	Homo sapiens
E431A	exhibits very similar expression levels and purification yields as the wild-type, but abolishes the proteolytic activity	Homo sapiens
H450A	shows an increase in proteolytic activity as compared with the wild-type	Homo sapiens
S456A	exhibits very similar expression levels and purification yields as the wild-type, but abolishes the proteolytic activity	Homo sapiens
S456A/D444V	low levels of residual activity	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
diisopropyl fluorophosphate	fully inhibits activity of the C-term protein	Homo sapiens
diisopropyl fluorophosphate	DLD is fully inactivated by 1 mM	Mus musculus
diisopropyl fluorophosphate	DLD is fully inactivated by 1 mM	Sus scrofa

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	-	Mus musculus	5739	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-
Mus musculus	-	C57BL6 male mice	-
Sus scrofa	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
by gel filtration	Mus musculus
wild-type DLD and mutants purified by nickel affinity chromatography. C-term DLD purified to near homogeneity by a five-step procedure	Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining
heart	-	Sus scrofa	-
liver	-	Mus musculus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
lipoamide + NADH	-	Homo sapiens	dihydrolipoamide + NAD+	-	?
mature frataxin + NADH	cleavage by C-term DLD	Mus musculus	denoted frataxin + NAD+	-	?
mature frataxin + NADH	cleavage by C-term DLD	Homo sapiens	denoted frataxin + NAD+	-	?
mature frataxin + NADH	exhibits DLD activity but is proteolytically inactive against mature frataxin. Purified pig DLD preparation exhibits weak but clear proteolytic activity	Sus scrofa	denoted frataxin + NAD+	-	?

Synonyms

Synonyms	Comment	Organism
dihydrolipoamide dehydrogenase	-	Mus musculus
dihydrolipoamide dehydrogenase	-	Homo sapiens
dihydrolipoamide dehydrogenase	-	Sus scrofa
DLD	-	Mus musculus
DLD	-	Homo sapiens
DLD	-	Sus scrofa

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.00196	-	-	Homo sapiens	diisopropyl fluorophosphate

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Release 2023.1 (January 2023)