Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Disulfiram | CAS 97-77-8, reaction of disulfiram with protein thiol groups by formation of a mixed disulfide or formation of an intra-molecular disulfide resulting in conformational changes. Inactivation under pseudo-first order conditions occurs in a time- and dose-dependent manner. In the absence of disulfiram, but in the presence of 2% methanol as DSF vehicle, no changes in enzymatic activities are observed. Using a DSF concentration range 10-30 microM, inactivation kinetics were biphasic with rate constants differing in one order of magnitude, and inactivation partial. The residual activity at infinite time, decreases as the disulfiram concentrations increases, reaching a value near zero at 30 microM disulfiram, whereas the amplitude of the two inactivation phases increases, each one reaching about 50% of initial activity at 30 microM disulfiram. | Sus scrofa |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
230000 | - |
for the homotetramer | Sus scrofa |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sus scrofa | - |
- |
- |
Purification (Comment) | Organism |
---|---|
the protein undergoes several chromatographic and dialysis steps during purification | Sus scrofa |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+ | catalyzes the last irreversible step in the synthesis of the osmoprotector glycine betaine | Sus scrofa |
Renatured (Comment) | Organism |
---|---|
2-mercaptoethanol, Reactivation of DSF-inactivated enzyme with 10 mM 2-mercaptoethanol | Sus scrofa |
DTT, Reactivation of disulfiram-inactivated enzyme with 5 mM DTT | Sus scrofa |
GSH, Reactivation of DSF-inactivated with 10 mM GSH | Sus scrofa |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
kidney | localized in cortex and medulla cells | Sus scrofa | - |
Subunits | Comment | Organism |
---|---|---|
homotetramer | - |
Sus scrofa |
Synonyms | Comment | Organism |
---|---|---|
BADH | - |
Sus scrofa |
betaine aldehyde dehydrogenase | - |
Sus scrofa |
betaine aldehyde: NAD+ oxidoreductase | - |
Sus scrofa |
pkBADH | - |
Sus scrofa |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | protective effects of NAD+ against inactivation of BADH by disulfiram | Sus scrofa | |
NADP+ | - |
Sus scrofa |