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Literature summary 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

EC Number Activating Compound Comment Organism Structure
1.8.1.4 Guanidine-HCl 4°C: activates the enzyme 2.5fold at 0.2 M Geobacillus stearothermophilus
1.8.1.4 KCl 4°C: activates the enzyme at concentrations below 1 M Geobacillus stearothermophilus
1.8.1.4 additional information no activation by urea Geobacillus stearothermophilus
1.8.1.4 NaCl 4°C: activates the enzyme at concentrations below 1 M Geobacillus stearothermophilus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.8.1.4 Guanidine-HCl 4°C: 50% inactivation at 1.0 M, complete inactivation at 1.6 M, reversible Geobacillus stearothermophilus

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.4 Geobacillus stearothermophilus
-
-
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
1.8.1.4 inactivation of the enzyme by guanidine-HCl is reversible by its removal Geobacillus stearothermophilus

Synonyms

EC Number Synonyms Comment Organism
1.8.1.4 dihydrolipoamide dehydrogenase
-
 Geobacillus stearothermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.4 FAD the cofactor is released from the enzyme with guanidine-HCl at concentration above 2 M forming inactive aggregates Geobacillus stearothermophilus