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 | 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 (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 | 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 | 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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Mus musculus | 5739 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Mus musculus | - |
C57BL6 male mice | - |
Sus scrofa | - |
- |
- |
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 | Comment | Organism | Textmining |
---|---|---|---|
heart | - |
Sus scrofa | - |
liver | - |
Mus musculus | - |
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 | 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 Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.00196 | - |
- |
Homo sapiens | diisopropyl fluorophosphate |