Literature summary extracted from
Incharoensakdi, A.; Hibino, T.; Takabe, T.
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
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
1.2.1.8 |
glycine betaine |
activates the wild-type enzyme but not the mutant enzyme |
Spinacia oleracea |
|
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.2.1.8 |
mutant enzyme E103Q expressed in Escherichia coli |
Spinacia oleracea |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
1.2.1.8 |
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
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
1.2.1.8 |
(NH4)2SO4 |
mutant enzyme is less sensitive to inhibition than wild-type enzyme |
Spinacia oleracea |
|
1.2.1.8 |
choline |
mutant enzyme shows stronger inhibition compared to wild-type enzyme |
Spinacia oleracea |
|
1.2.1.8 |
Isovaleraldehyde |
wild-type enzyme shows stronger inhibition than the mutant enzyme |
Spinacia oleracea |
|
1.2.1.8 |
NaCl |
mutant enzyme is slightly more sensitive to inhibition than wild-type enzyme |
Spinacia oleracea |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.2.1.8 |
Spinacia oleracea |
- |
- |
- |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.2.1.8 |
BADH |
- |
Spinacia oleracea |
1.2.1.8 |
betaine aldehyde dehydrogenase |
- |
Spinacia oleracea |
Temperature Stability [°C]
EC Number |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Comment |
Organism |
---|
1.2.1.8 |
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
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
1.2.1.8 |
additional information |
- |
mutant enzyme E103Q exhibits a broader temperature optimum than the wild-type enzyme |
Spinacia oleracea |
pH Stability
EC Number |
pH Stability |
pH Stability Maximum |
Comment |
Organism |
---|
1.2.1.8 |
5 |
11 |
mutant enzyme is less stable than the wild-type enzyme in the pH-range 5-11 |
Spinacia oleracea |