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Literature summary 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.
    View publication on PubMedView publication on EuropePMC

Activating Compound

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

Application

EC Number Application Comment Organism
1.8.1.4 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)

EC Number Cloned (Comment) Organism
1.8.1.4 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

EC Number Protein Variants Comment Organism
1.8.1.4 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
1.8.1.4 E431A exhibits very similar expression levels and purification yields as the wild-type, but abolishes the proteolytic activity Homo sapiens
1.8.1.4 H450A shows an increase in proteolytic activity as compared with the wild-type Homo sapiens
1.8.1.4 S456A exhibits very similar expression levels and purification yields as the wild-type, but abolishes the proteolytic activity Homo sapiens
1.8.1.4 S456A/D444V low levels of residual activity Homo sapiens

Inhibitors

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

Localization

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

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.1.4 by gel filtration Mus musculus
1.8.1.4 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

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.4 lipoamide + NADH
-
 Homo sapiens dihydrolipoamide + NAD+
-
 ?
1.8.1.4 mature frataxin + NADH cleavage by C-term DLD Mus musculus denoted frataxin + NAD+
-
 ?
1.8.1.4 mature frataxin + NADH cleavage by C-term DLD Homo sapiens denoted frataxin + NAD+
-
 ?
1.8.1.4 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

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

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.8.1.4 0.00196
-
-
 Homo sapiens diisopropyl fluorophosphate