Inhibitors | Comment | Organism | Structure |
---|---|---|---|
K+ | thermal stability of the pkBADH-NAD+ complex in the presence of K+ shows a complete loss of the ellipticity signal and highly cooperative thermal transitions in each thermogram in the presence of each K+ concentration tested. In all tested conditions, the thermal denaturation is irreversible | Sus scrofa | |
NADH | a mixed-type inhibitor of the enzyme. After NADH release, the enzyme cannot start a new catalytic cycle, possibly because of the catalytic residue protonation state | Sus scrofa |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | pkBADH kinetic analysis | Sus scrofa |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
K+ | required for binding of cofactor NAD+. K+ causes small changes in secondary and tertiary structures that influences the active site conformation, binding of K+ to the enzyme caused changes in the alpha-helix content of 4% and 12% in the presence of 25 mM and 100 mM K+, respectively | Sus scrofa |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
betaine aldehyde + NAD+ + H2O | Sus scrofa | - |
betaine + NADH + 2 H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sus scrofa | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+ | porcine kidney BADH follows an iso bi-bi ordered mechanism in which NAD+ is the first substrate to bind to pkBADH and NADH is the last product released | Sus scrofa |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
kidney | - |
Sus scrofa | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
betaine aldehyde + NAD+ + H2O | - |
Sus scrofa | betaine + NADH + 2 H+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | secondary and tertiary structure of pkBADH in presence or absence of NAD+, fluorescence quenching spectra of pkBADH titrated with variable NAD+ concentrations in presence of potassium, overview. The deconvolution data analysis shows a 13% increase in the pkBADH helical structure, a decrease of 7% in beta-sheet content and 6% in turns content during the pkBADH-NAD+ complex formation | Sus scrofa |
Synonyms | Comment | Organism |
---|---|---|
BADH | - |
Sus scrofa |
betaine aldehyde dehydrogenase | - |
Sus scrofa |
pkBADH | - |
Sus scrofa |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Sus scrofa |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
47.2 | 59.9 | thermal stability of the pkBADH-NAD+ complex in the presence of K+ shows a complete loss of the ellipticity signal and highly cooperative thermal transitions in each thermogram in the presence of each K+ concentration tested. In all tested conditions, the thermal denaturation is irreversible. The first derivative analysis from the pkBADH-NAD+ complex shows a peak with a (Tm)app value of 47.2°C, the addition of 25 mM K+ increased the (Tm)app to 59.9°C, while the addition of 50 mM or 100 mM K+ provokes changes in the (Tm)app to 55.9°C or 54.9°C, respectively. Binding of NAD+ to pkBADH causes a lower thermal stability of the enzyme | Sus scrofa |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Sus scrofa |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | porcine kidney betaine aldehyde dehydrogenase (pkBADH) binds NAD+ with different affinities at each active site and the binding is K+ dependent | Sus scrofa |
General Information | Comment | Organism |
---|---|---|
physiological function | porcine kidney betaine aldehyde dehydrogenase (pkBADH) binds NAD+ with different affinities at each active site and the binding is K+ dependent | Sus scrofa |