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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
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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