Cloned (Comment) | Organism |
---|---|
gene BADH, sequence comparisons, recombinant expression of the enzyme in Escherichia coli strain ER2566 | Sus scrofa |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | thermodynamcis | Sus scrofa |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
K+ | presence of K+ stabilizes the enzyme secondary structure and maintains its alpha-helix content. K+ increases the thermal stability of the pkBADHNAD+ complex by 5.3°C | Sus scrofa |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
224000 | - |
recombinant enzyme, gel filtration | Sus scrofa |
232000 | - |
recombinant enzyme, native PAGE | 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 | A0A6M5K8J2 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme from Escherichia coli strain ER2566 by chitin affinity chromatography | 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 | enzyme secondary structrue analysis, pkBADH/NAD+ interaction analysis by circular dichroism (CD) and by isothermal titration calorimetry (ITC) by titrating the enzyme with NAD+, overview. pkBADH shows 17% of unordered structure, 41% of alpha-helix, and 29% of beta-sheet | Sus scrofa |
tetramer | 4 * 53940, about, sequence calculation, 4 * 54000, recombinant enzyme, SDS-PAGE | 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 |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Sus scrofa |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | pkBADH/NAD+ interaction analysis by circular dichroism (CD) and by isothermal titration calorimetry (ITC) by titrating the enzyme with NAD+ | Sus scrofa |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Sus scrofa | sequence calculation | - |
5.85 |
General Information | Comment | Organism |
---|---|---|
additional information | pkBADH/NAD+ interaction analysis by circular dichroism (CD) and by isothermal titration calorimetry (ITC) by titrating the enzyme with NAD+. Binding of NAD+ to the enzyme causes changes in its secondary structure, the presence of K+ helps maintain its alpha-helix content. BADH enzyme structure homology modeing using the human ALDH9A1 structure (HsALDH9A1, PDB ID 6QAK) as template. The conserved catalytic residues C288, G285, N157, and E254 and the decapeptide VTLELGGKSP are identified | Sus scrofa |