Literature summary for 1.8.1.4 extracted from
Hiromasa, Y.; Meno, K.; Aso, Y.
Denaturation of the Bacillus stearothermophilus dihydrolipoamide dehydrogenase in the presence of guanidine-HCl at low temperature (2003), J. Fac. Agric. Kyushu Univ., 47, 387-394.
No PubMed abstract available
Activating Compound
Activating Compound |
Comment |
Organism |
Structure |
Guanidine-HCl |
4°C: activates the enzyme 2.5fold at 0.2 M |
Geobacillus stearothermophilus |
|
KCl |
4°C: activates the enzyme at concentrations below 1 M |
Geobacillus stearothermophilus |
|
additional information |
no activation by urea |
Geobacillus stearothermophilus |
|
NaCl |
4°C: activates the enzyme at concentrations below 1 M |
Geobacillus stearothermophilus |
|
Inhibitors
Inhibitors |
Comment |
Organism |
Structure |
Guanidine-HCl |
4°C: 50% inactivation at 1.0 M, complete inactivation at 1.6 M, reversible |
Geobacillus stearothermophilus |
|
Organism
Organism |
UniProt |
Comment |
Textmining |
Geobacillus stearothermophilus |
- |
- |
- |
Renatured (Commentary)
Renatured (Comment) |
Organism |
inactivation of the enzyme by guanidine-HCl is reversible by its removal |
Geobacillus stearothermophilus |
Synonyms
Synonyms |
Comment |
Organism |
dihydrolipoamide dehydrogenase |
- |
Geobacillus stearothermophilus |
Cofactor
Cofactor |
Comment |
Organism |
Structure |
FAD |
the cofactor is released from the enzyme with guanidine-HCl at concentration above 2 M forming inactive aggregates |
Geobacillus stearothermophilus |
|