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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.
    View publication on PubMed

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
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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