EC Number   |
Metals/Ions |
Reference |
|---|
    1.2.1.8 | Ca2+ |
increase of concentration from 0 to 0.00075 mM produces a 2fold increase in activity |
390363 |
| 1.2.1.8 | Ca2+ |
results indicate that transgenic plants have a higher Ca2+ accumulation than the wild type under saline conditions |
688198 |
| 1.2.1.8 | Cl- |
BADH plays an important role in the tolerance of plants to salinity |
689664 |
| 1.2.1.8 | Cl- |
results indicate that transgenic plants have a lower Cl- accumulation than the wild type under saline conditions |
688198 |
| 1.2.1.8 | Cl- |
treatment of seedlings after germinating with 6.25-200 mmol/l |
686072 |
| 1.2.1.8 | K+ |
- |
695893, 699567 |
| 1.2.1.8 | K+ |
activation up to 0.15 M, decreases activity at higher concentrations |
390329 |
| 1.2.1.8 | 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 |
763372 |
| 1.2.1.8 | 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 |
763411 |
| 1.2.1.8 | K+ |
required for maintenance of its active conformation. At low concentrations, the enzyme is totally inactivated upon removal of K+. NAD+ protects against inactivation by absence of K+, betaine aldehyde affords partial protection. NH4+ but not Na+ can mimic the effect of K+. At pH 7.0 in the absence of K+ in a buffer of low ionic strength, the active tetrameric form dissociates into inactive monomers |
655204 |
