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Literature summary for 1.2.1.8 extracted from
- Glu103Gln site-directed mutation causes an alteration in physical properties of spinach betaine aldehyde dehydrogenase (2002), J. Biochem. Mol. Biol. Biophys., 6, 243-248.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| glycine betaine | activates the wild-type enzyme but not the mutant enzyme | Spinacia oleracea |  |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| mutant enzyme E103Q expressed in Escherichia coli | Spinacia oleracea |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E103Q | mutant enzyme is slightly more sensitive to inhibition by NaCl but less sensitive to inhibition by (NH4)2SO4. Glycine betaine activates the wild-type enzyme but not the mutant enzyme. Mutant enzyme shows stronger inhibition by choline compared to wild-type enzyme. Wild-type enzyme shows stronger inhibition by isovaleraldehyde than the mutant enzyme.Mutant enzyme exhibits a broader temperature optimum than the wild-type enzyme. Mutant enzyme appears to be more heat labile than the wild-type enzyme. Mutant enzyme is less stable than the wild-type enzyme in the pH-range 5-11. Mutant enzyme and wild-type enzyme are protected by NAD+ against thermal inactivation in a similar manner. Neither glycine betaine nor NaCl can afford protection against thermal inactivation in the mutant enzyme whereas some protection is observed in the wild-type enzyme | Spinacia oleracea |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| (NH4)2SO4 | mutant enzyme is less sensitive to inhibition than wild-type enzyme | Spinacia oleracea | |
| choline | mutant enzyme shows stronger inhibition compared to wild-type enzyme | Spinacia oleracea | |
| Isovaleraldehyde | wild-type enzyme shows stronger inhibition than the mutant enzyme | Spinacia oleracea | |
| NaCl | mutant enzyme is slightly more sensitive to inhibition than wild-type enzyme | Spinacia oleracea | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Spinacia oleracea | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BADH | - |
Spinacia oleracea |
| betaine aldehyde dehydrogenase | - |
Spinacia oleracea |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
mutant enzyme E103Q appears to be more heat labile than the wild-type enzyme. Mutant enzyme E103Q and wild-type enzyme are protected by NAD+ against thermal inactivation in a similar manner. Neither glycine betaine nor NaCl can afford protection against thermal inactivation in the mutant enzyme whereas some protection is observed in the wild-type enzyme | Spinacia oleracea |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
mutant enzyme E103Q exhibits a broader temperature optimum than the wild-type enzyme | Spinacia oleracea |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 11 | mutant enzyme is less stable than the wild-type enzyme in the pH-range 5-11 | Spinacia oleracea |
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