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1,3-diaminopropane + NAD+ + H2O
?
-
-
-
-
?
3-aminopropionaldehyde + NAD(P)+ + H2O
?
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropanoate + NADH + H+
-
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionic acid + NADH + H+
3-aminopropionaldehyde + NAD+ + H2O
?
3-dimethylsulfoniopropionaldehyde + NAD(P)+ + H2O
?
-
-
-
?
3-dimethylsulfoniopropionaldehyde + NAD+ + H2O
?
-
-
-
-
?
3-dimethylsulfoniopropionaldehyde + NAD+ + O2
3-dimethylsulfoniopropionate + NADH
-
steady state bi bi mechanism with ordered addition of substrates and random release of products
-
-
ir
3-N-trimethylaminopropionaldehyde + NAD+ + H2O
3-N-trimethylaminopropanoate + NADH + H+
-
-
-
-
?
3-N-trimethylaminopropionaldehyde + NAD+ + H2O
3-N-trimethylaminopropionate + NADH + H+
-
-
-
-
?
3-N-trimethylaminopropionaldehyde + NAD+ + H2O
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH + 2 H+
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH + H+
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
4-gamma-aminobutyraldehyde + NAD+ + H2O
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutyrate + NADH + H+
-
-
-
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
?
4-N-trimethylaminobutyraldehyde + NAD(P)+ + H2O
?
-
-
-
?
4-N-trimethylaminobutyraldehyde + NAD+ + H2O
4-N-trimethylaminobutyrate + NADH + H+
-
-
-
-
?
4-N-trimethylaminobutyraldehyde + NAD+ + H2O
4-N-trmethylaminobutanoate + NADH + H+
-
-
-
-
?
4-N-trimethylaminobutyraldehyde + NAD+ + H2O
?
4-trimethylaminobutyraldehyde + NAD+ + H2O
3-trimethylaminobutyrate + NADH
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
-
-
-
?
aminoacetaldehyde + NAD+ + H2O
aminoacetate + NADH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
-
-
-
-
?
betaine aldehyde + NAD(P)+ + H2O
betaine + NAD(P)H + H+
-
-
-
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + 2 H+
-
-
-
-
ir
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
betaine aldehyde + NAD+ + H2O
betaine + NADH
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + 2 H+
-
-
-
r
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
betaine aldehyde + NADP+ + H2O
betaine + NADPH
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
betaine aldehyde + NADP+ + H2O
glycine betaine + NADPH + H+
-
-
-
ir
butyraldehyde + NAD+ + H2O
butyrate + NADH
-
at 40% of the activity with betaine aldehyde
-
-
?
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
-
-
-
-
?
butyraldehyde + NADP+ + H2O
butyrate + NADPH + H+
-
-
-
-
?
DL-glyceraldehyde + NAD+ + H2O
glycerate + NADH + H+
-
-
-
-
?
DL-glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
-
-
-
?
formaldehyde + NADP+ + H2O
formate + NADPH + H+
-
-
-
-
?
gamma-aminobutyraldehyde + NAD(P)+ + H2O
?
-
-
-
?
glyceraldehyde + NAD+ + H2O
glycerate + NADH
-
at 30% of the activity with betaine aldehyde
-
-
?
glycine betaine aldehyde + NAD+ + H2O
glycine betaine + NADH
-
-
-
-
?
glycine betaine aldehyde + NADP+ + H2O
glycine betaine + NADPH
-
-
-
-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH
glycolaldehyde + NAD+ + H2O
glycolate + NADH + H+
-
-
-
-
?
glycolaldehyde + NADP+ + H2O
glycolate + NADPH + H+
-
-
-
-
?
isovaleraldehyde + NAD+ + H2O
isovalerate + NADH + H+
-
-
-
-
?
isovaleraldehyde + NADP+ + H2O
isovalerate + NADPH + H+
-
-
-
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
-
-
-
?
methylglyoxal + NADP+ + H2O
? + NADPH + H+
-
-
-
-
?
N-acetyl-4-aminobutyraldehyde + NAD+ + H2O
?
-
-
-
-
?
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoate + NADH + H+
-
-
-
-
?
p-nitrobenzaldehyde + NADP+ + H2O
p-nitrobenzoate + NADPH + H+
-
-
-
-
?
phenyl acetaldehyde + NAD+ + H2O
phenyl acetate + NADH + H+
-
-
-
-
?
phenyl acetaldehyde + NADP+ + H2O
phenyl acetate + NADPH + H+
-
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH
-
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
-
-
-
?
propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
-
-
-
-
?
undecanal + NAD+ + H2O
undecanoate + NADH + H+
-
-
-
-
?
undecanal + NADP+ + H2O
undecanoate + NADPH + H+
-
-
-
-
?
valeraldehyde + NAD+ + H2O
valerate + NADH + H+
-
-
-
-
?
valeraldehyde + NADP+ + H2O
valerate + NADPH + H+
-
-
-
-
?
additional information
?
-
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
-
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionic acid + NADH + H+
-
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionic acid + NADH + H+
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
?
-
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
?
-
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
?
-
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
?
-
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
?
-
-
-
-
?
3-N-trimethylaminopropionaldehyde + NAD+ + H2O
?
-
-
-
-
?
3-N-trimethylaminopropionaldehyde + NAD+ + H2O
?
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
-
no activity
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
-
-
-
?
4-gamma-aminobutyraldehyde + NAD+ + H2O
?
-
-
-
-
?
4-gamma-aminobutyraldehyde + NAD+ + H2O
?
-
-
-
-
?
4-gamma-aminobutyraldehyde + NAD+ + H2O
?
-
-
-
-
?
4-gamma-aminobutyraldehyde + NAD+ + H2O
?
-
-
-
-
?
4-gamma-aminobutyraldehyde + NAD+ + H2O
?
-
-
-
-
?
4-gamma-aminobutyraldehyde + NAD+ + H2O
?
-
-
-
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
?
-
-
-
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
?
-
-
-
-
?
4-N-trimethylaminobutyraldehyde + NAD+ + H2O
?
-
-
-
-
?
4-N-trimethylaminobutyraldehyde + NAD+ + H2O
?
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
at 20% of the activity with betaine aldehyde
-
-
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
-
-
-
-
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
-
-
-
-
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
-
-
-
ir
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
-
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
enzyme catalyzes the final irreversible step in the synthesis of glycine betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
Amaranthus sp.
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
the enzyme is involved in the metabolism of choline, induced during growth on choline
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
the enzyme is involved in the metabolism of choline, induced during growth on choline
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
highly specific for betaine aldehyde
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
enzyme of the osmoregulatory choline-glycine betaine pathway
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
the salt tolerance is an essential property for the enzyme participating in the cellular synthesis of an osmoprotectant
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
reverse reaction not detected
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
preferentially uses NADP+ over NAD+
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
enzyme catalyzes the last, irreversible step in the synthesis of the osmoprotectant glycine betaine from choline, also obligatory step in the assimilation of carbon and nitrogen when bacteria are growing in choline or choline precursors
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
inducible enzyme accumulates in the presence of choline, acetylcholine or betaine in the medium
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
reverse reaction not detected
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
inducible enzyme accumulates in the presence of choline, acetylcholine or betaine in the medium
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
the enzyme has an important function in the metabolism of choline to betaine, a major osmolyte. Betaine is also important in mammalian organisms as a major methyl group donor and nitrogen source
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
the age-related acceleration in conversion of choline into betaine probably tends to diminish unesterified choline concentrations
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
enzyme is induced several-fold by salinization
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
equilibrium of the reaction strongly favours betaine formation
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
enzyme is induced several-fold by salinization
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
last step in betaine synthesis, a nontoxic or protective osmolyte under saline or dry conditions
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
accumulation of betaine is a strategy of plants to survive drought, salinity, and extreme temperatures
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Vallaris sp.
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Q53CF4
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
regulates osmotic pressure and protects enzyme activities; the transgenic plants have a higher accumulation of betaine
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
the enzyme catalyzes the second step in the synthesis of the osmoprotectant glycine betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
the osmoprotective compound glycine betaine is produced from choline by two enzymes. Choline dehydrogenase oxidizes choline to betaine aldehyde and then further to glycine betaine, while betaine aldehyde dehydrogenase facilitates the conversion of betaine aldehyde to glycine betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
more active on medium-chain aldehydes than on betaine aldehyde
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
belongs to the NAD-dependent dehydrogenase family, characterized by the typical aldehyde substrate binding domain
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
barley plants synthesize GB through catalytic reaction of the functional BADH protein, even though a large number of incorrectly processed BADH transcripts observed may considerably reduce the precise gene.
-
ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
barley plants synthesize glycine betaine through catalytic reaction of the functional BADH protein, even though a large number of incorrectly processed BADH transcripts observe in this study may considerably reduce the precise gene
-
ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
glycine betaine is not only an nontoxic osmoprotectant but also maintains protein and membrane conformations under various stress conditions
-
ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
the appropriate level of glycine betaine may be regulated at both the transcriptional and posttranscriptional levels. Namely, the transcription is induced abundantly in response to the osmotic stresses, while the proper amount of precise gene products is balanced by posttranscriptional processing
-
ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
the appropriate level of glycine may be regulated at both the transcriptional and posttranscriptional levels; namely, the transcription is induced abundantly in response to the osmotic stresses, while the proper amount of precise gene products is balanced by posttranscriptional processing
-
ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
Results demonstrate that accumulation of glycine betaine in vivo in the chloroplast in tobacco plants by introducing the BADH gene for betaine aldehyde dehydrogenase from spinach resulted in increased tolerance of growth of young seedlings to salt stress. Furthermore results demonstrate that accumulation of glycine betaine in vivo leads to increased tolerance of CO2 assimilation to salt stress.
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
accumulated in many species in response to salt stress. It protects the cell by maintaining an osmotic balance with the environment and by stabilizing quaternary structure of complex proteins
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
glycine betaine synthesis; two-step oxidation involving choline monooxygenase and BADH
recombinant yeasts transformed with the two genes CMO and BADH exhibited higher tolerance to salt, methanol and high temperature stress.
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
-
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
-
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
NAD+ is preferred over NADP+
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
-
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
preferentially uses NADP+ over NAD+
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
no activity with NAD+
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
-
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
no activity with NAD+
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
75% of the activity with NAD+
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
25% of the maximal activity with NAD+
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
-
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
-
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
-
more active on medium-chain aldehydes than on betaine aldehyde
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
-
low activity with NADP+
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
-
-
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
-
-
-
ir
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
-
the enzyme has evolved a complex mechanism, involving several conformational rearrangements of the active site, to suit the reactivity of the essential thiol to the availability of dinucleotide and sunstrate
-
-
ir
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
the enzyme is also active with NADP+, but the NAD-supported activity is at least 10times higher
-
-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH
-
-
-
-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH
-
-
-
-
?
additional information
?
-
-
no activity with succinic semialdehyde
-
-
?
additional information
?
-
Halalkalibacterium halodurans
enzyme BADH is active with choline as substrate and phenazine methosulfate as primary electron acceptor producing measurable O2 (reaction of EC 1.14.15.7)
-
-
-
additional information
?
-
Halalkalibacterium halodurans SMBPL06
enzyme BADH is active with choline as substrate and phenazine methosulfate as primary electron acceptor producing measurable O2 (reaction of EC 1.14.15.7)
-
-
-
additional information
?
-
the enzyme is also active with 4-aminobutyraldehyde and 3-aminopropionaldehyde, EC 1.2.1.19
-
-
-
additional information
?
-
2-acetyl-1-pyrroline, the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele badh2-E7, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
2-acetyl-1-pyrroline, the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele badh2-E7, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
2-acetyl-1-pyrroline, the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele badh2-E7, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
-
2-acetyl-1-pyrroline, the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele badh2-E7, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
2-acetyl-1-pyrroline; the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele, badh2-E2, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
2-acetyl-1-pyrroline; the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele, badh2-E2, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
2-acetyl-1-pyrroline; the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele, badh2-E2, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
-
2-acetyl-1-pyrroline; the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele, badh2-E2, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. Because the absence of BADH2 protein results in fragrance, this suggests that Badh2 is not directly involved in biosynthesis. Alternative possibilities to explain the effect of BADH2 are that the BADH2 enzyme is involved in a competing pathway in which one of the 2-acetyl-1-pyrroline precursors serves as a BADH2 substrate or that BADH2 participates in 2-acetyl-1-pyrroline catabolism. The intact 503 amino acid BADH2 encoded by the complete Badh2 gene inhibits 2-acetyl-1-pyrroline biosynthesis by converting 4-aminobutyraldehyde to gamma-aminobutyric acid, whereas the absence of BADH2 due to nonfunctional badh2 alleles results in AB-ald accumulation and thus turns on the pathway toward 2-acetyl-1-pyrroline biosynthesis.
-
-
?
additional information
?
-
dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. Because the absence of BADH2 protein results in fragrance, this suggests that Badh2 is not directly involved in biosynthesis. Alternative possibilities to explain the effect of BADH2 are that the BADH2 enzyme is involved in a competing pathway in which one of the 2-acetyl-1-pyrroline precursors serves as a BADH2 substrate or that BADH2 participates in 2-acetyl-1-pyrroline catabolism. The intact 503 amino acid BADH2 encoded by the complete Badh2 gene inhibits 2-acetyl-1-pyrroline biosynthesis by converting 4-aminobutyraldehyde to gamma-aminobutyric acid, whereas the absence of BADH2 due to nonfunctional badh2 alleles results in AB-ald accumulation and thus turns on the pathway toward 2-acetyl-1-pyrroline biosynthesis.
-
-
?
additional information
?
-
dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. Because the absence of BADH2 protein results in fragrance, this suggests that Badh2 is not directly involved in biosynthesis. Alternative possibilities to explain the effect of BADH2 are that the BADH2 enzyme is involved in a competing pathway in which one of the 2-acetyl-1-pyrroline precursors serves as a BADH2 substrate or that BADH2 participates in 2-acetyl-1-pyrroline catabolism. The intact 503 amino acid BADH2 encoded by the complete Badh2 gene inhibits 2-acetyl-1-pyrroline biosynthesis by converting 4-aminobutyraldehyde to gamma-aminobutyric acid, whereas the absence of BADH2 due to nonfunctional badh2 alleles results in AB-ald accumulation and thus turns on the pathway toward 2-acetyl-1-pyrroline biosynthesis.
-
-
?
additional information
?
-
-
dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. Because the absence of BADH2 protein results in fragrance, this suggests that Badh2 is not directly involved in biosynthesis. Alternative possibilities to explain the effect of BADH2 are that the BADH2 enzyme is involved in a competing pathway in which one of the 2-acetyl-1-pyrroline precursors serves as a BADH2 substrate or that BADH2 participates in 2-acetyl-1-pyrroline catabolism. The intact 503 amino acid BADH2 encoded by the complete Badh2 gene inhibits 2-acetyl-1-pyrroline biosynthesis by converting 4-aminobutyraldehyde to gamma-aminobutyric acid, whereas the absence of BADH2 due to nonfunctional badh2 alleles results in AB-ald accumulation and thus turns on the pathway toward 2-acetyl-1-pyrroline biosynthesis.
-
-
?
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
-
various other C3-C6 amino acids
-
-
?
additional information
?
-
-
isozyme BADH1 catalyzes the oxidation of acetaldehyde efficiently, while the activity of isozyme BADH2 is extremely low
-
-
?
additional information
?
-
rice BADH1 and BADH2 show greater affinity (Km) and higher catalytic efficiency (kcat/ Km) towards amino aldehydes, such as gamma-aminobutyraldehyde (GABald) and gamma-guanidinobutyraldehyde (GGBald), in comparison with betaine aldehyde, cf. EC 1.2.1.19. BADH2 catalysis generates glycine betaine, whereas BADH1 is not able to catalyse glycine betaine formation
-
-
-
additional information
?
-
rice BADH1 and BADH2 show greater affinity (Km) and higher catalytic efficiency (kcat/ Km) towards amino aldehydes, such as gamma-aminobutyraldehyde (GABald) and gamma-guanidinobutyraldehyde (GGBald), in comparison with betaine aldehyde, cf. EC 1.2.1.19. BADH2 catalysis generates glycine betaine, whereas BADH1 is not able to catalyse glycine betaine formation
-
-
-
additional information
?
-
rice BADH1 and BADH2 show greater affinity (Km) and higher catalytic efficiency (kcat/ Km) towards amino aldehydes, such as gamma-aminobutyraldehyde (GABald) and gamma-guanidinobutyraldehyde (GGBald), in comparison with betaine aldehyde. BADH2 catalysis generates glycine betaine, whereas BADH1 is not able to catalyse glycine betaine formation
-
-
-
additional information
?
-
rice BADH1 and BADH2 show greater affinity (Km) and higher catalytic efficiency (kcat/ Km) towards amino aldehydes, such as gamma-aminobutyraldehyde (GABald) and gamma-guanidinobutyraldehyde (GGBald), in comparison with betaine aldehyde. BADH2 catalysis generates glycine betaine, whereas BADH1 is not able to catalyse glycine betaine formation
-
-
-
additional information
?
-
betaine aldehyde substrates docking study, overview. The enzyme shows a good affinity with both betaine aldehyde (BAD) and 4-aminobutyraldehyde (GABald) as substrates
-
-
-
additional information
?
-
-
betaine aldehyde substrates docking study, overview. The enzyme shows a good affinity with both betaine aldehyde (BAD) and 4-aminobutyraldehyde (GABald) as substrates
-
-
-
additional information
?
-
-
no activity with 3-dimethylsulfoniopropionaldehyde
-
-
?
additional information
?
-
BADH can also use as substrates aminoaldehydes and other quaternary ammonium and tertiary sulfonium compounds, thereby participating in polyamine catabolism and in the synthesis of gamma-aminobutyrate, carnitine, and 3-dimethylsulfoniopropionate
-
-
?
additional information
?
-
-
BADH can also use as substrates aminoaldehydes and other quaternary ammonium and tertiary sulfonium compounds, thereby participating in polyamine catabolism and in the synthesis of gamma-aminobutyrate, carnitine, and 3-dimethylsulfoniopropionate
-
-
?
additional information
?
-
-
betaine aldehyde dehydrogenase gene expression in leaves increases with salt stress
-
-
?
additional information
?
-
-
betaine aldehyde dehydrogenase gene expression in leaves increases with salt stress
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH + H+
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + 2 H+
-
-
-
-
ir
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
betaine aldehyde + NAD+ + H2O
betaine + NADH
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + 2 H+
-
-
-
r
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
betaine aldehyde + NADP+ + H2O
glycine betaine + NADPH + H+
-
-
-
ir
additional information
?
-
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
-
-
-
-
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
-
-
-
-
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
-
-
-
ir
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
-
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
enzyme catalyzes the final irreversible step in the synthesis of glycine betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
the enzyme is involved in the metabolism of choline, induced during growth on choline
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
the enzyme is involved in the metabolism of choline, induced during growth on choline
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
enzyme of the osmoregulatory choline-glycine betaine pathway
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
the salt tolerance is an essential property for the enzyme participating in the cellular synthesis of an osmoprotectant
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
enzyme catalyzes the last, irreversible step in the synthesis of the osmoprotectant glycine betaine from choline, also obligatory step in the assimilation of carbon and nitrogen when bacteria are growing in choline or choline precursors
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
inducible enzyme accumulates in the presence of choline, acetylcholine or betaine in the medium
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
inducible enzyme accumulates in the presence of choline, acetylcholine or betaine in the medium
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
the enzyme has an important function in the metabolism of choline to betaine, a major osmolyte. Betaine is also important in mammalian organisms as a major methyl group donor and nitrogen source
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
the age-related acceleration in conversion of choline into betaine probably tends to diminish unesterified choline concentrations
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
enzyme is induced several-fold by salinization
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
enzyme is induced several-fold by salinization
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
last step in betaine synthesis, a nontoxic or protective osmolyte under saline or dry conditions
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
accumulation of betaine is a strategy of plants to survive drought, salinity, and extreme temperatures
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Vallaris sp.
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Q53CF4
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
regulates osmotic pressure and protects enzyme activities; the transgenic plants have a higher accumulation of betaine
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
the enzyme catalyzes the second step in the synthesis of the osmoprotectant glycine betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
the osmoprotective compound glycine betaine is produced from choline by two enzymes. Choline dehydrogenase oxidizes choline to betaine aldehyde and then further to glycine betaine, while betaine aldehyde dehydrogenase facilitates the conversion of betaine aldehyde to glycine betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
belongs to the NAD-dependent dehydrogenase family, characterized by the typical aldehyde substrate binding domain
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
barley plants synthesize GB through catalytic reaction of the functional BADH protein, even though a large number of incorrectly processed BADH transcripts observed may considerably reduce the precise gene.
-
ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
barley plants synthesize glycine betaine through catalytic reaction of the functional BADH protein, even though a large number of incorrectly processed BADH transcripts observe in this study may considerably reduce the precise gene
-
ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
glycine betaine is not only an nontoxic osmoprotectant but also maintains protein and membrane conformations under various stress conditions
-
ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
the appropriate level of glycine betaine may be regulated at both the transcriptional and posttranscriptional levels. Namely, the transcription is induced abundantly in response to the osmotic stresses, while the proper amount of precise gene products is balanced by posttranscriptional processing
-
ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
the appropriate level of glycine may be regulated at both the transcriptional and posttranscriptional levels; namely, the transcription is induced abundantly in response to the osmotic stresses, while the proper amount of precise gene products is balanced by posttranscriptional processing
-
ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
Results demonstrate that accumulation of glycine betaine in vivo in the chloroplast in tobacco plants by introducing the BADH gene for betaine aldehyde dehydrogenase from spinach resulted in increased tolerance of growth of young seedlings to salt stress. Furthermore results demonstrate that accumulation of glycine betaine in vivo leads to increased tolerance of CO2 assimilation to salt stress.
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
accumulated in many species in response to salt stress. It protects the cell by maintaining an osmotic balance with the environment and by stabilizing quaternary structure of complex proteins
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
glycine betaine synthesis; two-step oxidation involving choline monooxygenase and BADH
recombinant yeasts transformed with the two genes CMO and BADH exhibited higher tolerance to salt, methanol and high temperature stress.
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
-
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
-
-
-
?
additional information
?
-
2-acetyl-1-pyrroline, the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele badh2-E7, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
2-acetyl-1-pyrroline, the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele badh2-E7, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
2-acetyl-1-pyrroline, the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele badh2-E7, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
-
2-acetyl-1-pyrroline, the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele badh2-E7, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
2-acetyl-1-pyrroline; the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele, badh2-E2, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
2-acetyl-1-pyrroline; the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele, badh2-E2, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
2-acetyl-1-pyrroline; the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele, badh2-E2, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
-
2-acetyl-1-pyrroline; the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele, badh2-E2, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. Because the absence of BADH2 protein results in fragrance, this suggests that Badh2 is not directly involved in biosynthesis. Alternative possibilities to explain the effect of BADH2 are that the BADH2 enzyme is involved in a competing pathway in which one of the 2-acetyl-1-pyrroline precursors serves as a BADH2 substrate or that BADH2 participates in 2-acetyl-1-pyrroline catabolism. The intact 503 amino acid BADH2 encoded by the complete Badh2 gene inhibits 2-acetyl-1-pyrroline biosynthesis by converting 4-aminobutyraldehyde to gamma-aminobutyric acid, whereas the absence of BADH2 due to nonfunctional badh2 alleles results in AB-ald accumulation and thus turns on the pathway toward 2-acetyl-1-pyrroline biosynthesis.
-
-
?
additional information
?
-
dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. Because the absence of BADH2 protein results in fragrance, this suggests that Badh2 is not directly involved in biosynthesis. Alternative possibilities to explain the effect of BADH2 are that the BADH2 enzyme is involved in a competing pathway in which one of the 2-acetyl-1-pyrroline precursors serves as a BADH2 substrate or that BADH2 participates in 2-acetyl-1-pyrroline catabolism. The intact 503 amino acid BADH2 encoded by the complete Badh2 gene inhibits 2-acetyl-1-pyrroline biosynthesis by converting 4-aminobutyraldehyde to gamma-aminobutyric acid, whereas the absence of BADH2 due to nonfunctional badh2 alleles results in AB-ald accumulation and thus turns on the pathway toward 2-acetyl-1-pyrroline biosynthesis.
-
-
?
additional information
?
-
dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. Because the absence of BADH2 protein results in fragrance, this suggests that Badh2 is not directly involved in biosynthesis. Alternative possibilities to explain the effect of BADH2 are that the BADH2 enzyme is involved in a competing pathway in which one of the 2-acetyl-1-pyrroline precursors serves as a BADH2 substrate or that BADH2 participates in 2-acetyl-1-pyrroline catabolism. The intact 503 amino acid BADH2 encoded by the complete Badh2 gene inhibits 2-acetyl-1-pyrroline biosynthesis by converting 4-aminobutyraldehyde to gamma-aminobutyric acid, whereas the absence of BADH2 due to nonfunctional badh2 alleles results in AB-ald accumulation and thus turns on the pathway toward 2-acetyl-1-pyrroline biosynthesis.
-
-
?
additional information
?
-
-
dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. Because the absence of BADH2 protein results in fragrance, this suggests that Badh2 is not directly involved in biosynthesis. Alternative possibilities to explain the effect of BADH2 are that the BADH2 enzyme is involved in a competing pathway in which one of the 2-acetyl-1-pyrroline precursors serves as a BADH2 substrate or that BADH2 participates in 2-acetyl-1-pyrroline catabolism. The intact 503 amino acid BADH2 encoded by the complete Badh2 gene inhibits 2-acetyl-1-pyrroline biosynthesis by converting 4-aminobutyraldehyde to gamma-aminobutyric acid, whereas the absence of BADH2 due to nonfunctional badh2 alleles results in AB-ald accumulation and thus turns on the pathway toward 2-acetyl-1-pyrroline biosynthesis.
-
-
?
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
-
betaine aldehyde dehydrogenase gene expression in leaves increases with salt stress
-
-
?
additional information
?
-
-
betaine aldehyde dehydrogenase gene expression in leaves increases with salt stress
-
-
?
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(NH4)2SO4
-
mutant enzyme is less sensitive to inhibition than wild-type enzyme
3-dimethylsulfoniopropionaldehyde
-
at high concentrations
5,5'-dithiobis[2-nitrobenzoic acid]
-
the effect of the thiol reagent DTNB on the native enzyme structure of the wild type enzyme and the mutants is examined
Acetylcholine
-
10 mM, 18% inhibition
AgNO3
-
3 mM, 90-100% inhibition
benzaldehyde
-
1 mM, 51% inhibition
benzyltrimethylamine iodide
-
10 mM, 45% inhibition
bis[diethylthiocarbamyl]disulfide
-
the effect of the thiol reagent disulfiram on the native enzyme structure of the wild type enzyme and the mutants is examined
Butyrylcholine
-
100 mM, 73% inhibition
cyclophosphamide
CTX, an antineoplastic and immuno-suppressant pre-drug, the enzyme loses 43% and 69% of its activity at 0.2 mM and 2.0 mM CTX, respectively, after 120 min. Docking of CTX to pkBADH and molecular modeling. The pseudofirst-order rate constant of inactivation (kobs) is dependent on CTX concentration only at low concentrations (0.2 and 0.6 mM CTX), and then the kobs between 1.0 and 2.0 mM show similar values. CTX can have access more easily to the catalytic cysteine when NAD+ opens the active site for substrate betaine aldehyde binding according to the kinetic mechanism, kinetics of inactivation of pkBADH by CTX in the presence of NADH, overview. Reversibility of inactivation, pkBADH inactivated with 2 mM CTX and incubated with DTT recovers 96% of its activity, and 93% with 2-mercaptoethanol, but in the presence of glutathione (GSH), the enzyme is not reactivated
ethanolamine
-
100 mM, 35% inhibition
Glutaraldehyde
-
10 mM, 83% inhibition
glyceraldehyde
-
100 mM, 83% inhibition
H2O2
-
more than 50% inhibition at 0.1 mM H2O2, noncompetitive inhibition with respect to NAD+ or to betaine aldehyde at saturating concentrations of the other substrate at pH 7.0 or 8.0
Isobutanal
-
10 mM, 93% inhibition
isopentanal
-
1 mM, 84% inhibition
Isovaleraldehyde
-
wild-type enzyme shows stronger inhibition than the mutant enzyme
methyl methanethiosulfonate
methyl methanethiosulphonate
-
pH-dependence of the second-order rate constant of inactivation suggests that at low pH values the essential Cys exists as thiolate by the formation of an ion pair with a positively charged residue
methyl(bis-beta-chloroethyl)amine
-
-
Mg2+
-
0.4 M, complete inhibition
N,N-dimethylethanolamine
-
100 mM, 57% inhibition
N,N-dimethylglycine
-
1 mM, 24% inhibition
n-butylaldehyde
-
10 mM, 96% inhibition
N-Methylethanolamine
-
100 mM, 50% inhibition
N-methylglycine
-
1 mM, 24% inhibition
NAD(P)H
reversible inactivation
NADP+
-
substrate inhibition above 10 mM
NADPH
-
product inhibition
phenylacetaldehyde
-
1 mM, 54% inhibition
S-methyl-N,N-diethyldithiocarbamoyl sulfone
most potent irreversible inhibition in vitro at 0.05 mM, but no inhibition in situ
S-methyl-N,N-diethyldithiocarbamoyl sulfoxide
irreversible inhibition
S-methyl-N,N-diethylthiocarbamoyl sulfone
irreversible inhibition
S-methyl-N,N-diethylthiocarbamoyl sulfoxide
-
S-methylmethanesulfonate
-
the effect of the thiol reagent MMTS on the native enzyme structure of the wild type enzyme and the mutants is examined
sodium meta-arsenite plus 2,3-dimercaptopropanol
-
arsenite-BAL
tetraethylamine iodide
-
10 mM, 19% inhibition
tetramethylamine iodide
-
10 mM, 19% inhibition
tetramethylammonium hydroxide
-
100 mM, 57% inhibition
tetrapropylamine iodide
-
10 mM, 43% inhibition
trimethylacetaldehyde
-
100 mM, 89% inhibition
1,10-phenanthroline
-
-
1,10-phenanthroline
-
no inhibition at 1 mM
2,2'-dipyridyl
-
-
2,2'-dipyridyl
-
no inhibition at 3 mM
acetaldehyde
-
100 mM, 83% inhibition
acetaldehyde
-
10 mM, 69% inhibition
AMP
-
competitive with respect to NAD+ and mixed with betaine aldehyde and uncompetitive with respect to NAD+
AMP
-
competitive with respect to NAD+ and mixed with betaine aldehyde
betaine
-
10 mM, 14% inhibition
betaine
-
product inhibition
Betaine aldehyde
-
0.5 mM, non-competitive inhibitor against NAD+
Betaine aldehyde
-
above 0.5 mM
Betaine aldehyde
-
the enzyme is reversibly and partially inactivated by betaine aldehyde in the absence of NAD+ in a time- and concentration-dependent mode
Betaine aldehyde
strongly inhibited by betaine aldehyde at concentrations of more than 0.15 mM
Betaine aldehyde
-
substrate inhibition at concentrations of betaine aldehyde as low as 0.15 mM
Betaine aldehyde
-
substrate inhibition
Ca2+
-
500 mM CaCl2, about 50% loss of activity
Ca2+
-
500 mM CaCl2, about 50% loss of activity
Ca2+
-
10 mM CaCl2, 90% inhibition
Ca2+
-
500 mM CaCl2, about 50% loss of activity
choline
-
-
choline
-
100 mM, 78% inhibition
choline
-
10 mM, 23% inhibition
choline
-
mutant enzyme shows stronger inhibition compared to wild-type enzyme
choline
-
competitive against betaine aldehyde and uncompetitive with respect to NAD+
cimetidine
-
-
Disulfiram
-
inactivates in a time- and dose-dependent manner, inactivation kinetics is biphasic with second-order inactivation rate constants at pH 7.5 of 6.8 per M per sec and 0.33 per M per sec, inactivation is faster in presence of NAD(P)+ than in absence, inactivation is increased by NAD(P)H and betaine aldehyde, reactivation by dithiothreitol, inactivation is reversible by glutathione
Disulfiram
-
inactivates in a time- and dose-dependent manner, inactivation kinetics is monophasic with a second-order inactivation rate constant at pH 6.0 of 4.9 per M per sec and at pH 8.8 of 1000 per M per sec, inactivation is faster in presence of NAD(P)+ than in absence, inactivation is protected by NAD(P)H and betaine aldehyde, reactivation by dithiothreitol, inactivation is reversible by glutathione
Disulfiram
-
CAS 97-77-8, reaction of disulfiram with protein thiol groups by formation of a mixed disulfide or formation of an intra-molecular disulfide resulting in conformational changes. Inactivation under pseudo-first order conditions occurs in a time- and dose-dependent manner. In the absence of disulfiram, but in the presence of 2% methanol as DSF vehicle, no changes in enzymatic activities are observed. Using a DSF concentration range 10-30 microM, inactivation kinetics were biphasic with rate constants differing in one order of magnitude, and inactivation partial. The residual activity at infinite time, decreases as the disulfiram concentrations increases, reaching a value near zero at 30 microM disulfiram, whereas the amplitude of the two inactivation phases increases, each one reaching about 50% of initial activity at 30 microM disulfiram.
glycine betaine
-
no inhibition up to 10 mM
glycine betaine
Amaranthus sp.
-
product inhibition
Hg2+
-
-
Hg2+
-
0.0001-0.0005 mM HgCl2
Hg2+
-
3 mM HgCl2, 90-100% inhibition
iodoacetamide
-
1 mM
iodoacetate
-
-
K+
-
1.0 mM, 35% inhibition
K+
-
thermal stability of the pkBADH-NAD+ complex in the presence of K+ shows a complete loss of the ellipticity signal and highly cooperative thermal transitions in each thermogram in the presence of each K+ concentration tested. In all tested conditions, the thermal denaturation is irreversible
methyl methanethiosulfonate
-
in absence of ligands, the kinetics of inactivation is biphasic, suggesting the existence of two enzyme conformers differing in the reactivity of their catalytic thiolate. Preincubation with NADH or betaine aldehyde prior to the chemical modification brings about active site rearrangements that result in an import decrease in the inactivation rate. Binding of NAD+ increases the rate of inactivation after prolonged preincubation
methyl methanethiosulfonate
-
in absence of ligands, the kinetics of inactivation is biphasic, suggesting the existence of two enzyme conformers differing in the reactivity of their catalytic thiolate. Preincubation with coenzyme or the aldehyde prior to the chemical modification brings about active site rearrangements that result in an import decrease in the inactivation rate
NaCl
In response to high salt stress conditions numerous truncated transcripts of two BADH homologs resulting from an unusual posttranscriptional processing are detected in barley. The observed events take place at the 5' exonic region, and lead to the insertion of exogenous gene sequences and a variety of deletions that result in the removal of translation initiation codon, loss of functional domain, and frameshifts with premature termination by introducing stop codon.; In response to high salt stress conditions numerous truncated transcripts of two BADH homologs resulting from an unusual posttranscriptional processing are detected in barley. The observed events take place at the 5' exonic region, and lead to the insertion of exogenous gene sequences and a variety of deletions that results in the removal of translation initiation codon, loss of functional domain, and frameshifts with premature termination by introducing stop codon.
NaCl
-
the activity of isoform BADH2 decreases at NaCl concentrations greater than 300 mM
NaCl
0.5 M, expression of OsBADH2 is increased under salt stress conditions, but at high concentrations, expression is inhibited.; 0.5 M, firstly, expression of OsBADH1 is increased under salt stress conditions, but at high concentrations, expression has been inhibited.
NaCl
-
inhibitory effect increases with concentrations from 50 mM to 250 mM
NaCl
-
0.5 M, 50% inhibition
NaCl
-
mutant enzyme is slightly more sensitive to inhibition than wild-type enzyme
NaCl
Yeast strains containing the BADH gene from Suaeda salsa were streaked on YPD medium supplemented with 0.5% methanol and different NaCl concentrations (0-1.5 mol/l). Salt tolerance is examined after incubation at 30°C for 3 days. Growth of yeast strains A764, A765, A767 and YPIC3 is severely suppressed containing 0.8 mol/l NaCl and completely inhibited on 1.0 mol/l NaCl without methanol induction. However, induced with 0.5% of methanol, A764, A765 and A767 grow well but YPIC3 is suppressed greatly on YPD medium containing 1.0 mol/l NaCl. A764, A765, and A767 can resist 1.2 mol/l NaCl and can grow a little on 1.5 mol/l NaCl with 0.5% of methanol induction.
NaCl
-
40% inhibition above 0.3 M
NaCl
at a concentration of 0.5 M, expression of BADH2 is inhibited
NaCl
Q53CF4
at a concentration of 0.5 M, expression of BADH1 is inhibited; at a concentration of 0.5 M, expression of BADH2 is inhibited
NaCl
100 mM about 70% activity to 500 mM about 40% activity; 100 mM about 70% activity to 500 mM about 40% activity; 100 mM about 70% activity to 500 mM about 40% activity; 100 mM about 70% activity to 500 mM about 40% activity; 100 mM about 70% activity to 500 mM about 40% activity; 100 mM about 70% activity to 500 mM about 40% activity; 100 mM about 70% activity to 500 mM about 40% activity; 100 mM about 70% activity to 500 mM about 40% activity; 100 mM about 70% activity to 500 mM about 40% activity
NAD+
Amaranthus sp.
-
glycerol favours substrate inhibition
NAD+
substrate inhibition by high concentrations of NAD+
NADH
-
mixed inhibitor against NAD+ and betaine aldehyde
NADH
-
product inhibition
NADH
-
mixed inhibited against NAD+ and betaine aldehyde
NADH
-
a mixed-type inhibitor of the enzyme. After NADH release, the enzyme cannot start a new catalytic cycle, possibly because of the catalytic residue protonation state
NH4+
-
-
NH4+
-
above 0.4 M, more than 60% inhibition
PCMB
-
-
ZnCl2
-
0.0001-0.0005 mM
ZnCl2
-
3 mM, 90-100% inhibition
additional information
Amaranthus sp.
-
no product inhibition
-
additional information
-
no substrate inhibition with NAD+
-
additional information
diethyldithiocarbamic acid does not inactivate the enzyme in vitro and in situ
-
additional information
-
diethyldithiocarbamic acid does not inactivate the enzyme in vitro and in situ
-
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0.00000054 - 3.7
3-aminopropionaldehyde
0.0027
3-dimethylsulfoniopropionaldehyde
-
-
0.035 - 0.34
3-N-trimethylaminopropionaldehyde
0.00196 - 1.1
4-Aminobutyraldehyde
0.000024 - 0.00005
4-guanidinobutyraldehyde
0.0078 - 0.041
4-N-trimethylaminobutyraldehyde
0.0014
4-trimethylaminobutyraldehyde
-
cytoplasmic enzyme
0.000005 - 14.8
Betaine aldehyde
11 - 48
D,L-glyceraldehyde
3.8
formaldehyde
-
pH 7.7, coenzyme NAD+
0.13
glycine betaine aldehyde
-
-
0.152 - 11.5
glycolaldehyde
0.2 - 15
Isovaleraldehyde
0.5
p-nitrobenzaldehyde
-
pH 7.7, coenzyme NAD+
51 - 140
phenyl acetaldehyde
additional information
additional information
-
0.00000054
3-aminopropionaldehyde
-
pH 8.7, 37°C
0.0012
3-aminopropionaldehyde
-
isozyme BADH2, pH and temperature not specified in the publication
0.004
3-aminopropionaldehyde
-
0.017
3-aminopropionaldehyde
-
isozyme BADH1, pH and temperature not specified in the publication
0.453
3-aminopropionaldehyde
-
at pH 8.0 and 30°C
3.7
3-aminopropionaldehyde
in 100 mM sodium diphosphate pH 8.0, at 22°C
0.035
3-N-trimethylaminopropionaldehyde
-
isozyme BADH1, pH and temperature not specified in the publication
0.0914
3-N-trimethylaminopropionaldehyde
-
at pH 8.0 and 30°C
0.34
3-N-trimethylaminopropionaldehyde
-
isozyme BADH2, pH and temperature not specified in the publication
0.00196
4-Aminobutyraldehyde
-
at pH 8.0 and 30°C
0.003
4-Aminobutyraldehyde
-
wild-type enzyme
0.004
4-Aminobutyraldehyde
-
mitochondrial enzyme
0.005
4-Aminobutyraldehyde
-
-
0.0098
4-Aminobutyraldehyde
-
mutant enzyme E103Q
0.024
4-Aminobutyraldehyde
-
cytoplasmic enzyme
0.037
4-Aminobutyraldehyde
-
-
0.049
4-Aminobutyraldehyde
-
1.1
4-Aminobutyraldehyde
in 100 mM sodium diphosphate pH 8.0, at 22°C
0.000024
4-guanidinobutyraldehyde
-
pH 8.7, 37°C
0.00005
4-guanidinobutyraldehyde
-
pH 8.7, 37°C
0.0078
4-N-trimethylaminobutyraldehyde
-
isozyme BADH1, pH and temperature not specified in the publication
0.0221
4-N-trimethylaminobutyraldehyde
-
at pH 8.0 and 30°C
0.041
4-N-trimethylaminobutyraldehyde
-
isozyme BADH2, pH and temperature not specified in the publication
0.014
acetaldehyde
-
-
0.014
acetaldehyde
-
mitochondrial enzyme
0.115
acetaldehyde
-
cytoplasmic enzyme
0.13
acetaldehyde
-
isozyme BADH1, pH and temperature not specified in the publication
0.17
acetaldehyde
-
isozyme BADH2, pH and temperature not specified in the publication
3.6
acetaldehyde
-
pH 7.7, coenzyme NAD+
28
acetaldehyde
-
pH 7.7, coenzyme NADP+
0.1
benzaldehyde
-
pH 7.7, coenzyme NAD+
6.7
benzaldehyde
-
pH 7.7, coenzyme NADP+
0.000005
Betaine aldehyde
-
pH 8.7, 37°C
0.0561
Betaine aldehyde
-
-
0.065
Betaine aldehyde
-
mutant enzyme E103Q
0.068
Betaine aldehyde
-
wild-type enzyme
0.07716
Betaine aldehyde
-
-
0.09
Betaine aldehyde
mutant enzyme A441C, at pH 8.0 and 30°C
0.0937
Betaine aldehyde
-
-
0.098
Betaine aldehyde
wild type enzyme, at pH 8.0 and 30°C
0.109
Betaine aldehyde
-
at pH 8.0 and 30°C
0.11
Betaine aldehyde
-
-
0.11
Betaine aldehyde
-
mutant enzyme G234T, at pH 8.0 and 30°C
0.118
Betaine aldehyde
-
mitochondrial enzyme
0.119
Betaine aldehyde
mutant enzyme A441S, at pH 8.0 and 30°C
0.12
Betaine aldehyde
-
mutant enzyme G234A, at pH 8.0 and 30°C
0.123
Betaine aldehyde
-
cytoplasmic enzyme
0.127
Betaine aldehyde
-
-
0.133
Betaine aldehyde
-
-
0.1455
Betaine aldehyde
-
-
0.15
Betaine aldehyde
-
pH 7.5, 20°C, native betaine-aldehyde dehydrogenase or betaine aldehyde dehydrogenase/choline dehydrogenase fusion protein
0.16
Betaine aldehyde
-
-
0.17
Betaine aldehyde
at pH 8.0 and 30°C
0.17
Betaine aldehyde
-
wild type enzyme, at pH 8.0 and 30°C
0.17
Betaine aldehyde
-
mutant enzyme G234S, at pH 8.0 and 30°C
0.18
Betaine aldehyde
mutant enzyme A441T, at pH 8.0 and 30°C
0.208
Betaine aldehyde
-
-
0.23
Betaine aldehyde
-
isozyme BADH2, pH and temperature not specified in the publication
0.26
Betaine aldehyde
-
-
0.26
Betaine aldehyde
-
mutant enzyme H448F, at pH 8.0 and 30°C
0.31
Betaine aldehyde
-
-
0.38
Betaine aldehyde
-
-
0.434
Betaine aldehyde
-
30°C, pH 8.0, cosubstrate NADP+
0.506
Betaine aldehyde
-
30°C, pH 8.0, cosubstrate NAD+
0.512
Betaine aldehyde
mutant enzyme A441V, at pH 8.0 and 30°C
0.57
Betaine aldehyde
-
mutant enzyme H448F/P449M, at pH 8.0 and 30°C
0.605
Betaine aldehyde
mutant enzyme A441F, at pH 8.0 and 30°C
0.665
Betaine aldehyde
pH 8.0, 30°C, recombinant isozyme LrAMADH1
0.91
Betaine aldehyde
-
mutant enzyme Q162M, at pH 8.0 and 30°C
1.18
Betaine aldehyde
-
mutant enzyme H448F/Y450L, at pH 8.0 and 30°C
1.791
Betaine aldehyde
mutant enzyme A441I, at pH 8.0 and 30°C
1.8
Betaine aldehyde
-
pH 7.7, coenzyme NADP+
1.92
Betaine aldehyde
-
mutant enzyme Y450L, at pH 8.0 and 30°C
1.94
Betaine aldehyde
-
mutant enzyme P449M/Y450L, at pH 8.0 and 30°C
2.16
Betaine aldehyde
-
mutant enzyme L161M7Q162M, at pH 8.0 and 30°C
2.6
Betaine aldehyde
-
isozyme BADH1, pH and temperature not specified in the publication
4.61
Betaine aldehyde
-
mutant enzyme H448F/P449M/Y450L, at pH 8.0 and 30°C
4.76
Betaine aldehyde
-
mutant enzyme V288D, at pH 8.0 and 30°C
6.5
Betaine aldehyde
-
pH 7.7, coenzyme NAD+
6.81
Betaine aldehyde
in 100 mM sodium diphosphate pH 8.0, at 22°C
13.8
Betaine aldehyde
-
mutant enzyme S290T, at pH 8.0 and 30°C
14.8
Betaine aldehyde
-
mutant enzyme W456H, at pH 8.0 and 30°C
0.5
Butyraldehyde
-
pH 7.7, coenzyme NAD+
3.4
Butyraldehyde
-
pH 7.7, coenzyme NADP+
11
D,L-glyceraldehyde
-
pH 7.7, coenzyme NADP+
48
D,L-glyceraldehyde
-
pH 7.7, coenzyme NAD+
0.152
glycolaldehyde
-
mitochondrial enzyme
4.3
glycolaldehyde
-
pH 7.7, coenzyme NAD+
11.5
glycolaldehyde
-
pH 7.7, coenzyme NADP+
0.2
Isovaleraldehyde
-
pH 7.7, coenzyme NAD+
15
Isovaleraldehyde
-
pH 7.7, coenzyme NADP+
2.5
methylglyoxal
-
pH 7.7, coenzyme NAD+
9
methylglyoxal
-
pH 7.7, coenzyme NADP+
0.0025
NAD+
-
pH 7.7, reaction with benzaldehyde
0.0028
NAD+
mutant enzyme A441I, at pH 8.0 and 30°C
0.004
NAD+
-
pH 7.7, reaction with isovaleraldehyde
0.0064
NAD+
mutant enzyme A441V, at pH 8.0 and 30°C
0.00766
NAD+
-
at pH 8.0 and 30°C
0.009
NAD+
-
pH 7.7, reaction with undecanal
0.011
NAD+
-
reaction with betaine aldehyde
0.012
NAD+
-
pH 7.7, reaction with valeraldehyde
0.0133
NAD+
-
reaction with 3-dimethylsulfoniopropionaldehyde
0.014
NAD+
mutant enzyme A441C, at pH 8.0 and 30°C
0.018
NAD+
mutant enzyme A441F, at pH 8.0 and 30°C
0.019
NAD+
-
wild-type enzyme, reaction with betaine aldehyde
0.022
NAD+
wild type enzyme, at pH 8.0 and 30°C
0.023
NAD+
-
mutant enzyme E103Q, reaction with betaine aldehyde
0.024
NAD+
-
mutant enzyme E103Q, reaction with 4-aminobutyraldehyde
0.024
NAD+
mutant enzyme A441T, at pH 8.0 and 30°C
0.026
NAD+
-
wild-type enzyme, reaction with 4-aminopropionaldehyde
0.028
NAD+
-
cytoplasmic enzyme
0.029
NAD+
mutant enzyme A441S, at pH 8.0 and 30°C
0.034
NAD+
-
mitochondrial enzyme
0.05
NAD+
-
pH 7.7, reaction with phenyl acetaldehyde
0.083
NAD+
-
30°C, pH 8.0
0.12
NAD+
-
mutant enzyme G234S, at pH 8.0 and 30°C
0.136
NAD+
-
reaction with 4-aminobutyraldehyde
0.26
NAD+
-
wild type enzyme, at pH 8.0 and 30°C
0.27
NAD+
-
mutant enzyme V288D, at pH 8.0 and 30°C
0.3
NAD+
-
mutant enzyme G234T, at pH 8.0 and 30°C
0.34
NAD+
-
mutant enzyme H448F/Y450L, at pH 8.0 and 30°C
0.38
NAD+
-
mutant enzyme W456H, at pH 8.0 and 30°C
0.41
NAD+
-
mutant enzyme S290T, at pH 8.0 and 30°C
0.42
NAD+
-
mutant enzyme H448F, at pH 8.0 and 30°C
0.43
NAD+
at pH 8.0 and 30°C
0.43
NAD+
-
mutant enzyme P449M/Y450L, at pH 8.0 and 30°C
0.68
NAD+
-
mutant enzyme Q162M, at pH 8.0 and 30°C
0.71
NAD+
-
mutant enzyme L161M7Q162M, at pH 8.0 and 30°C
0.8
NAD+
-
pH 7.7, reaction with p-nitrobenzaldehyde
1.01
NAD+
-
mutant enzyme Y450L, at pH 8.0 and 30°C
1.12
NAD+
-
mutant enzyme G234A, at pH 8.0 and 30°C
1.12
NAD+
-
mutant enzyme H448F/P449M, at pH 8.0 and 30°C
3.42
NAD+
-
mutant enzyme H448F/P449M/Y450L, at pH 8.0 and 30°C
0.08
NADP+
-
pH 7.7, reaction with undecanal
0.27
NADP+
-
pH 7.7, reaction with valeraldehyde
0.31
NADP+
-
pH 7.7, reaction with isovaleraldehyde
0.385
NADP+
-
30°C, pH 8.0
0.61
NADP+
-
pH 7.7, reaction with phenyl acetaldehyde
1
NADP+
-
pH 7.7, reaction with p-nitrobenzaldehyde
1.4
NADP+
-
pH 7.7, reaction with benzaldehyde
2.26
NADP+
at pH 8.0 and 30°C
3.68
NADP+
-
at pH 8.0 and 30°C
51
phenyl acetaldehyde
-
pH 7.7, coenzyme NADP+
140
phenyl acetaldehyde
-
pH 7.7, coenzyme NAD+
0.8
propionaldehyde
-
pH 7.7, coenzyme NAD+
21
propionaldehyde
-
pH 7.7, coenzyme NADP+
2 - 3
Undecanal
-
pH 7.7, coenzyme NADP+
106
Undecanal
-
pH 7.7, coenzyme NAD+
0.2
Valeraldehyde
-
pH 7.7, coenzyme NAD+
4.1
Valeraldehyde
-
pH 7.7, coenzyme NADP+
additional information
additional information
-
for the mutants and wild-type enzymes KM NADP+ varies within 0.060 and 0.107 mM, KM NAD+ within 0.254 and 0.411 mM, KM betaine aldehyde within 0.270 and 0.434 mM
-
additional information
additional information
Michaelis-Menten kinetics, except for LrAMADH1 on 4-aminobutyraldehyde
-
additional information
additional information
-
pkBADH kinetic analysis
-
additional information
additional information
thermodynamcis
-
additional information
additional information
-
thermodynamcis
-
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evolution
all BADHs known have cysteine in the active site involved in the aldehyde binding, whereas the porcine kidney enzyme (pkBADH) also has a neighborhood cysteine, both sensitive to oxidation
malfunction
Q53CF4
some truncated transcripts of BADH are present in several crops. Such truncated transcripts may cause the accumulation of 2AP (2-acetyl-1-pyrroline), which is a key aroma compound. There is a possibility that inhibition of BADH function produces 2AP-based fragrance in main crops because of the existence of BADH isozymes
malfunction
some truncated transcripts of BADH are present in several crops. Such truncated transcripts may cause the accumulation of 2AP (2-acetyl-1-pyrroline), which is a key aroma compound. There is a possibility that inhibition of BADH function produces 2AP-based fragrance in main crops because of the existence of BADH isozymes
malfunction
some truncated transcripts of BADH are present in several crops. Such truncated transcripts may cause the accumulation of 2AP (2-acetyl-1-pyrroline), which is a key aroma compound. There is a possibility that inhibition of BADH function produces 2AP-based fragrance in main crops because of the existence of BADH isozymes
malfunction
some truncated transcripts of BADH are present in several crops. Such truncated transcripts may cause the accumulation of 2AP (2-acetyl-1-pyrroline), which is a key aroma compound. There is a possibility that inhibition of BADH function produces 2AP-based fragrance in main crops because of the existence of BADH isozymes
malfunction
-
some truncated transcripts of BADH are present in several crops. Such truncated transcripts may cause the accumulation of 2AP (2-acetyl-1-pyrroline), which is a key aroma compound. There is a possibility that inhibition of BADH function produces 2AP-based fragrance in main crops because of the existence of BADH isozymes. But the BADH transcripts from plant species such as Arabidopsis (Arabidopsis thaliana), spinach (Spinacia oleracea) and tomato (Solanum lycopersicum), correctly process the mRNA
malfunction
some truncated transcripts of BADH are present in several crops. Such truncated transcripts may cause the accumulation of 2AP (2-acetyl-1-pyrroline), which is a key aroma compound. There is a possibility that inhibition of BADH function produces 2AP-based fragrance in main crops because of the existence of BADH isozymes. But the BADH transcripts from plant species such as Arabidopsis (Arabidopsis thaliana), spinach (Spinacia oleracea) and tomato (Solanum lycopersicum), correctly process the mRNA
malfunction
some truncated transcripts of BADH are present in several crops. Such truncated transcripts may cause the accumulation of 2AP (2-acetyl-1-pyrroline), which is a key aroma compound. There is a possibility that inhibition of BADH function produces 2AP-based fragrance in main crops because of the existence of BADH isozymes. But the BADH transcripts from plant species such as Arabidopsis (Arabidopsis thaliana), spinach (Spinacia oleracea) and tomato (Solanum lycopersicum), correctly process the mRNA
malfunction
some truncated transcripts of BADH are present in several crops. Such truncated transcripts may cause the accumulation of 2AP (2-acetyl-1-pyrroline), which is a key aroma compound. There is a possibility that inhibition of BADH function produces 2AP-based fragrance in main crops because of the existence of BADH isozymes. Even though 2AP formation in Bassia latifolia occurs only in flowers (fleshy corolla), in fragrant rice and plants such as Pandanus amaryllifolius and Vallaris glabra, it exists in all aerial parts
malfunction
some truncated transcripts of BADH are present in several crops. Such truncated transcripts may cause the accumulation of 2AP (2-acetyl-1-pyrroline), which is a key aroma compound. There is a possibility that inhibition of BADH function produces 2AP-based fragrance in main crops because of the existence of BADH isozymes. Even though 2AP formation in Bassia latifolia occurs only in flowers (fleshy corolla), in fragrant rice and plants such as Pandanus amaryllifolius and Vallaris glabra, it exists in all aerial parts
malfunction
-
some truncated transcripts of BADH are present in several crops. Such truncated transcripts may cause the accumulation of 2AP (2-acetyl-1-pyrroline), which is a key aroma compound. There is a possibility that inhibition of BADH function produces 2AP-based fragrance in main crops because of the existence of BADH isozymes. Even though 2AP formation in Bassia latifolia occurs only in flowers (fleshy corolla), in fragrant rice and plants such as Pandanus amaryllifolius and Vallaris glabra, it exists in all aerial parts
malfunction
Vallaris sp.
-
some truncated transcripts of BADH are present in several crops. Such truncated transcripts may cause the accumulation of 2AP (2-acetyl-1-pyrroline), which is a key aroma compound. There is a possibility that inhibition of BADH function produces 2AP-based fragrance in main crops because of the existence of BADH isozymes. Even though 2AP formation in Bassia latifolia occurs only in flowers (fleshy corolla), in fragrant rice and plants such as Pandanus amaryllifolius and Vallaris glabra, it exists in all aerial parts
metabolism
-
betaine aldehyde dehydrogenase 2 is a key enzyme in the synthesis of fragrance aroma compounds. The extremely low activity of the enzyme in catalyzing the oxidation of acetaldehyde is crucial for the accumulation of the volatile compound 2-acetyl-1-pyrroline in fragrant rice
metabolism
in higher plants, glycine betaine (GB) is synthesized by two-step oxidation of choline. The first step is catalyzed by ferredoxin-dependent choline monooxygenase (CMO, EC 1.14.15.7) to produce betaine aldehyde (BAL). BAL is converted to GB by aminoaldehyde dehydrogenase (AMADH, EC 1.2.1.19) containing the activities of betaine aldehyde dehydrogenase (BADH)
metabolism
NO's involvement in the biosynthetic pathway of GB production in plants takes place prior to the involvement of BADH in converting the toxic intermediate betaine aldehyde to GB. The extent of the impact of NO on GB content and BADH activity also varies with light exposure, but the pattern observed is similar to that observed in dark-grown seedlings
physiological function
-
BADH1 is possibly involved in acetaldehyde oxidation in rice plant peroxisomes
physiological function
-
betaine aldehyde dehydrogenase gene BADH2 is associated with the fragrant phenotype in rice
physiological function
-
the badh2 gene alone is not sufficient enough to explain the genetic and molecular basis of fragrance in rice
physiological function
ALDH10A8 serves as detoxification enzyme controlling the level of aminoaldehydes, which are produced in cellular metabolism under stress conditions
physiological function
-
expression of the BADH gene in sweet potato increases enzyme activity and glycine betaine in these transgenic sweet potato plants, which subsequently improves their tolerance to multiple abiotic stresses including salt, oxidative stress, and low temperature by induction or activation reactive oxygen species scavenging and the accumulation of proline
physiological function
LDH10A9 serves as detoxification enzymes controlling the level of aminoaldehydes, which are produced in cellular metabolism under stress conditions
physiological function
-
overexpression of the betaine aldehyde dehydrogenase gene in transgenic trifoliate orange enhances salt stress tolerance and leads to accumulation of higher levels of glycine betaine
physiological function
the enzyme plays a role in salt (400 mM NaCl) and other osmotic stresses tolerance
physiological function
expression of the gene significantly enhances tolerance of Arabidopsis mutants to high salt and drought stresses
physiological function
the betaine aldehyde dehydrogenase gene substantially affects the phagocytic pathway in human phagocytes and in host cells in mice. The enzyme is involved in the bacterial adherent ability to phagocytes and is responsible for the bacterial persistence and virulence in mice
physiological function
-
the enzyme is a positive regulator during the response to NaCl
physiological function
the enzyme is involved in the cellular response of crustaceans to variations in environmental salinity
physiological function
the enzyme plays a crucial role in adaption of Ammopiptanthus nanus to heat (55°C) and salt (700 mM NaCl) stresses
physiological function
-
the enzyme plays a role in temperature stress tolerance
physiological function
betaine aldehyde dehydrogenase (BADH) is a key enzyme in glycine betaine (GB) synthesis, and the activity of the enzyme is significantly increased when plants are under abiotic stress, thus greatly increasing the accumulation of glycine betaine
physiological function
betaine aldehyde dehydrogenase (BADH) is an important gene for enhancing plants stress tolerance and productivity, overview. Betaine aldehyde dehydrogenase (BADH) is one of the important genes involved in the biosynthetic pathway of gylcine betaine (GB), and its introduction leads to an increased tolerance to a variety of abiotic stresses in different plant species
physiological function
betaine aldehyde dehydrogenase (BADH) is an important gene for enhancing plants stress tolerance and productivity, overview. Betaine aldehyde dehydrogenase (BADH) is one of the important genes involved in the biosynthetic pathway of gylcine betaine (GB), and its introduction leads to an increased tolerance to a variety of abiotic stresses in different plant species
physiological function
betaine aldehyde dehydrogenase (BADH) is an important gene for enhancing plants stress tolerance and productivity, overview. Betaine aldehyde dehydrogenase (BADH) is one of the important genes involved in the biosynthetic pathway of gylcine betaine (GB), and its introduction leads to an increased tolerance to a variety of abiotic stresses in different plant species
physiological function
betaine aldehyde dehydrogenase (BADH) is an important gene for enhancing plants stress tolerance and productivity, overview. Betaine aldehyde dehydrogenase (BADH) is one of the important genes involved in the biosynthetic pathway of gylcine betaine (GB), and its introduction leads to an increased tolerance to a variety of abiotic stresses in different plant species
physiological function
betaine aldehyde dehydrogenase (BADH) is an important gene for enhancing plants stress tolerance and productivity, overview. Betaine aldehyde dehydrogenase (BADH) is one of the important genes involved in the biosynthetic pathway of gylcine betaine (GB), and its introduction leads to an increased tolerance to a variety of abiotic stresses in different plant species
physiological function
betaine aldehyde dehydrogenase (BADH) is an important gene for enhancing plants stress tolerance and productivity, overview. Betaine aldehyde dehydrogenase (BADH) is one of the important genes involved in the biosynthetic pathway of gylcine betaine (GB), and its introduction leads to an increased tolerance to a variety of abiotic stresses in different plant species
physiological function
-
betaine aldehyde dehydrogenase (BADH) is an important gene for enhancing plants stress tolerance and productivity, overview. Betaine aldehyde dehydrogenase (BADH) is one of the important genes involved in the biosynthetic pathway of gylcine betaine (GB), and its introduction leads to an increased tolerance to a variety of abiotic stresses in different plant species
physiological function
-
betaine aldehyde dehydrogenase (BADH) leads to production of glycine betaine through the oxidation of betaine aldehyde. BADH is considered a key regulator for glycine betaine formation. Critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses. The BADH gene plays a multifunctional role in plants, detailed overview. It is an important factor in fragrance production, abiotic stresses and antibiotic-free selection of transgenic plants. By providing glycine betaine as a chemical interface, there is a critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses, e.g. drought stress, soil salinity stress, submergence stress, and temperature stress
physiological function
Q53CF4
betaine aldehyde dehydrogenase (BADH) leads to production of glycine betaine through the oxidation of betaine aldehyde. BADH is considered a key regulator for glycine betaine formation. Critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses. The BADH gene plays a multifunctional role in plants, detailed overview. It is an important factor in fragrance production, abiotic stresses and antibiotic-free selection of transgenic plants. By providing glycine betaine as a chemical interface, there is a critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses, e.g. drought stress, soil salinity stress, submergence stress, and temperature stress
physiological function
betaine aldehyde dehydrogenase (BADH) leads to production of glycine betaine through the oxidation of betaine aldehyde. BADH is considered a key regulator for glycine betaine formation. Critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses. The BADH gene plays a multifunctional role in plants, detailed overview. It is an important factor in fragrance production, abiotic stresses and antibiotic-free selection of transgenic plants. By providing glycine betaine as a chemical interface, there is a critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses, e.g. drought stress, soil salinity stress, submergence stress, and temperature stress
physiological function
betaine aldehyde dehydrogenase (BADH) leads to production of glycine betaine through the oxidation of betaine aldehyde. BADH is considered a key regulator for glycine betaine formation. Critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses. The BADH gene plays a multifunctional role in plants, detailed overview. It is an important factor in fragrance production, abiotic stresses and antibiotic-free selection of transgenic plants. By providing glycine betaine as a chemical interface, there is a critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses, e.g. drought stress, soil salinity stress, submergence stress, and temperature stress
physiological function
betaine aldehyde dehydrogenase (BADH) leads to production of glycine betaine through the oxidation of betaine aldehyde. BADH is considered a key regulator for glycine betaine formation. Critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses. The BADH gene plays a multifunctional role in plants, detailed overview. It is an important factor in fragrance production, abiotic stresses and antibiotic-free selection of transgenic plants. By providing glycine betaine as a chemical interface, there is a critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses, e.g. drought stress, soil salinity stress, submergence stress, and temperature stress
physiological function
betaine aldehyde dehydrogenase (BADH) leads to production of glycine betaine through the oxidation of betaine aldehyde. BADH is considered a key regulator for glycine betaine formation. Critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses. The BADH gene plays a multifunctional role in plants, detailed overview. It is an important factor in fragrance production, abiotic stresses and antibiotic-free selection of transgenic plants. By providing glycine betaine as a chemical interface, there is a critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses, e.g. drought stress, soil salinity stress, submergence stress, and temperature stress
physiological function
betaine aldehyde dehydrogenase (BADH) leads to production of glycine betaine through the oxidation of betaine aldehyde. BADH is considered a key regulator for glycine betaine formation. Critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses. The BADH gene plays a multifunctional role in plants, detailed overview. It is an important factor in fragrance production, abiotic stresses and antibiotic-free selection of transgenic plants. By providing glycine betaine as a chemical interface, there is a critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses, e.g. drought stress, soil salinity stress, submergence stress, and temperature stress
physiological function
betaine aldehyde dehydrogenase (BADH) leads to production of glycine betaine through the oxidation of betaine aldehyde. BADH is considered a key regulator for glycine betaine formation. Critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses. The BADH gene plays a multifunctional role in plants, detailed overview. It is an important factor in fragrance production, abiotic stresses and antibiotic-free selection of transgenic plants. By providing glycine betaine as a chemical interface, there is a critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses, e.g. drought stress, soil salinity stress, submergence stress, and temperature stress
physiological function
betaine aldehyde dehydrogenase (BADH) leads to production of glycine betaine through the oxidation of betaine aldehyde. BADH is considered a key regulator for glycine betaine formation. Critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses. The BADH gene plays a multifunctional role in plants, detailed overview. It is an important factor in fragrance production, abiotic stresses and antibiotic-free selection of transgenic plants. By providing glycine betaine as a chemical interface, there is a critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses, e.g. drought stress, soil salinity stress, submergence stress, and temperature stress
physiological function
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betaine aldehyde dehydrogenase (BADH) leads to production of glycine betaine through the oxidation of betaine aldehyde. BADH is considered a key regulator for glycine betaine formation. Critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses. The BADH gene plays a multifunctional role in plants, detailed overview. It is an important factor in fragrance production, abiotic stresses and antibiotic-free selection of transgenic plants. By providing glycine betaine as a chemical interface, there is a critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses, e.g. drought stress, soil salinity stress, submergence stress, and temperature stress
physiological function
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betaine aldehyde dehydrogenase (BADH) leads to production of glycine betaine through the oxidation of betaine aldehyde. BADH is considered a key regulator for glycine betaine formation. Critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses. The BADH gene plays a multifunctional role in plants, detailed overview. It is an important factor in fragrance production, abiotic stresses and antibiotic-free selection of transgenic plants. By providing glycine betaine as a chemical interface, there is a critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses, e.g. drought stress, soil salinity stress, submergence stress, and temperature stress
physiological function
Vallaris sp.
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betaine aldehyde dehydrogenase (BADH) leads to production of glycine betaine through the oxidation of betaine aldehyde. BADH is considered a key regulator for glycine betaine formation. Critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses. The BADH gene plays a multifunctional role in plants, detailed overview. It is an important factor in fragrance production, abiotic stresses and antibiotic-free selection of transgenic plants. By providing glycine betaine as a chemical interface, there is a critical role of BADH in enhancing the tolerance in an extensive range of plants subjected to different destructive abiotic stresses, e.g. drought stress, soil salinity stress, submergence stress, and temperature stress
physiological function
betaine aldehyde dehydrogenase 2 (BADH2) plays a key role in the accumulation of 2-acetyl-1-pyrroline (2AP), a fragrant compound in rice (Oryza sativa). BADH2 catalyses the oxidation of aminoaldehydes to carboxylic acids. But the inactive BADH2 is known to promote fragrance in rice
physiological function
isozyme LrAMADH1 shows low betaine aldehyde dehydrogenase activity, but is proved as bona fide BADH, which involves in glycine betaine (GB) synthesis in planta and responds to salt stress in Lycium ruthenicum plants
physiological function
nitric oxide and light co-regulate glycine betaine (GB) homeostasis in sunflower seedling cotyledons by modulating betaine aldehyde dehydrogenase transcript levels and activity. A reasonable amount of GB is being constitutively synthesized in sunflower seedling cotyledons. Sensing of NaCl stress, however, enhances the GB concentration by several folds. Analysis of GB accumulation at three different growth stages of seedling cotyledons (2, 4, and 6 days old) shows that accumulation is age dependent. NaCl stress and availability of NO regulate BADH activity and, therefore, accumulation of GB
physiological function
Pandanus amaryllifolius accumulates the highest concentration of the major basmati aroma volatile 2-acetyl-1-pyrroline (2AP) in the plant kingdom. The expression of 2AP is correlated with the presence of a nonfunctional betaine aldehyde dehydrogenase 2 (BADH2) in aromatic rice and other plant species. 2AP biosynthesis in Pandanus amaryllifolius is not due to the inactivation of BADH2
physiological function
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porcine kidney betaine aldehyde dehydrogenase (pkBADH) binds NAD+ with different affinities at each active site and the binding is K+ dependent
physiological function
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the betaine aldehyde dehydrogenase gene substantially affects the phagocytic pathway in human phagocytes and in host cells in mice. The enzyme is involved in the bacterial adherent ability to phagocytes and is responsible for the bacterial persistence and virulence in mice
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additional information
for Ile445 containing AMADHs, the existence of Asn290 rather than Thr290 leads to detectable BADH activity
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
additional information
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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
additional information
the 3D dimeric structure of BADH2 is modeled using homology modeling. Each monomer comprises of 3 domains (substrate-binding, NAD+-binding, and oligomerization domains). The NAD+-binding domain is the most mobile. A scissor-like motion is observed between the monomers. Inside the binding pocket, N162 and E260 are tethered by strong hydrogen bonds to residues in close proximity. In contrast, the catalytic C294 is very mobile and interacts occasionally with N162. The flexibility of the nucleophilic C294 can facilitate the attack of free carbonyl on an aldehyde substrate. Mainly, N162, E260, C294 are found to play a role in catalytic activity. C294 and E260 are involved in a key step of hemithioacetal-enzyme formation, while N162 helps stabilize an intermediate. Molecular dynamics (MD) simulations of substrate-bound enzyme. Both N162 and C294 form different degrees of hydrogen bonds. C294 seems to weakly hydrogen bond with adjacent amino acids (below 1% of hydrogen bonds with N162), whereas N162 forms a strong hydrogen bond with Q292 (over90%). Apparently, C294 seems to be flexible, whilst N162 is tethered by Q292 inside a pocket. The catalytic C294 is located in the middle of a cavity. The high flexibility of C294 which supports the role of the nucleophile C294's ability to attack a free carbonyl group of a bound substrate. On the contrary, N162 and E260 appear to be rigid due to strong interactions with their neighbours. Such interactions tethering N162 and E260 may help to shape a suitable environment for a catalytic activity
additional information
three-dimensional docking analysis of PaBADH2 with betaine aldehyde
additional information
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three-dimensional docking analysis of PaBADH2 with betaine aldehyde
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C439S
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steady-state kinetic and structure not significantly affected, stability severely reduced
C439V
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steady-state kinetic and structure not significantly affected, stability severely reduced
A441F
the mutant shows no activity with betaine aldehyde
A441S
the mutant exhibits slightly reduced activity with betaine aldehyde
A441T
the mutant exhibits clearly reduced activity with betaine aldehyde
A441V
the mutant shows no activity with betaine aldehyde
C450S
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the mutant is not inhibited by betaine aldehyde
E103K
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mutant enzyme has no activity with betaine aldehyde and 4-aminobutyraldehyde
G234A
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the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
G234T
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the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
H448F
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the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
H448F/P449M
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the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
H448F/P449M/Y450L
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the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
H448F/Y450L
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the mutant demonstrates a complete loss of substrate inhibition
L161M/Q162M
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the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
P449M/Y450L
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the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
Q162M
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the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
S290T
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the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
V288D
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the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
W456H
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the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
Y450L
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the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
C286A
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cysteine 286 plays an important role in the maintenance ot the tetrameric structure
C286A
mutant with reduced reactivity
C353A
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cysteine 353 not essential for enzyme activity
C353A
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steady-state kinetic and structure not significantly affected
C353A
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mutant, shows similar inactivation kinetics to the wild-type enzyme
C377A
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cysteine 377 not essential for enzyme activity
C377A
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steady-state kinetic and structure not significantly affected
C377A
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mutant, shows similar inactivation kinetics to the wild-type enzyme
C439A
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cysteine 439 not essential for enzyme activity
C439A
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steady-state kinetic and structure not significantly affected, stability severely reduced
C439A
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mutant, shows similar inactivation kinetics to the wild-type enzyme
A441C
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the mutant demonstrates reduced substrate inhibition by betaine aldehyde
A441C
the mutant exhibited almost wild type activity with betaine aldehyde
A441I
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the mutant demonstrates reduced substrate inhibition by betaine aldehyde
A441I
the mutant shows no activity with betaine aldehyde
E103Q
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Km-values for 4-aminobutyraldehyde increases compared to wild-type
E103Q
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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
G234S
the mutant shows increased activity and reduced substrate inhibition compared to the wild type enzyme
G234S
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the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
additional information
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transgenic expression of the enzyme in Arabidopsis thaliana to reduce salinity and drought stresses results in improved survival rate, fresh weight, relative water content, proline content, relative electrolyte leakage, MDA content root length, glycine betaine content, and RELs
additional information
recombinant expression in transgenic potato and in Populus nigra plants to reduce salinity stress results in improved proline and chlorophyll content, H2O2 and MDA levels, and in improved content of chlorophyll b, and SOD activity, respectively. Recombinant expression in transgenic Glcine max plants to reduce drought stress results in improved germination index, proline content, and POX activity
additional information
recombinant expression of AcBADH in transgenic Glycine max cv. Jinong 17 plants: the rate of germination is higher in the AcBADH transgenic lines than in Jinong 17, the BADH transgenic soybean lines also have longer roots than Jinong 17 under osmotic stress conditions. The primary root growth of AcBADH transgenic seedlings is stronger than that of wild-type. These results further demonstrate the AcBADH transgenic lines have increased tolerance to osmotic stress compared to the control. The BADH-transgenic lines exhibit a 1.6fold increase in glycine betaine (GB) content compared to the control, and thus have a significantly higher GB level. The transgenic plants also show highly increased drought resistance compared to wild-type. Phenotype of transgenic plants, overview
additional information
glycine betaine (GB) accumulation in transgenic crops following heterologous overexpression of the BADH gene dramatically improves the tolerance to salt, cold, and oxidative stresses. The root system of transgenic maize is more developed than that of wild-type maize, and the data showed the dry root weight of transgenic maize increased compared with the wild-type. The drought tolerance of high-generation BADH transgenic maize inbred lines at different growth stages using the hyperosmotic solution and water-withholding methods are analyzed. Molecular detection reveals that exogenous BADH is successfully introduced into the maize plant genome and overexpressed in three transgenic maize inbred lines. Under osmotic stress, transgenic maize hold better germination ability than the unmodified Dan988 wild-type line. In addition, transgenic maize contain higher levels of antioxidant enzymes and osmotic regulatory substances compared with wild-type, and thus accumulate less harmful substances and this alleviates the negative effects of drought. Engineered line Dan988-BADH-4 shows the best tolerance, followed by Dan988-BADH-2 and Dan988-BADH-1 while wild-type ranks lowest. BADH overexpression in maize is beneficial for drought tolerance. The agronomic traits of transgenic maize are not affected by the overexpression of BADH
additional information
transgenic expression of the enzyme in Triticum aestivum to reduce salinity stress results in improved glycine betaine accumulation, chlorophyll and carotenoid contents, photosynthetic efficiency, and Ca2+-ATPase activity
additional information
transgenic expression of the enzyme in Cichorium intybus to reduce salinity and drought stresses results in improved K+/Na+ ratio, glycine betaine (GB) accumulation, MDA content, and chlorophyll content, transgenic expression of the enzyme in Triticum aestivum to reduce salinity stress results in improved GB accumulation, K+/Na+ ratio, and survival rates
additional information
several truncated or recombinant transcripts of BADH1 and BADH2 emerging from an unusual post-transcriptional process have been found in rice resulting in the insertion of exogenous gene sequences and different deletions leading to the elimination of the start codon, the loss of a functional domain and the introduction of a premature termination codon. Such a truncated BADH2 enzyme can lead to the accumulation of 2AP, the main fragrant compound
additional information
several truncated or recombinant transcripts of BADH1 and BADH2 emerging from an unusual post-transcriptional process have been found in rice resulting in the insertion of exogenous gene sequences and different deletions leading to the elimination of the start codon, the loss of a functional domain and the introduction of a premature termination codon. Non-aromatic rice cultivars comprise a functional BADH2 gene, while aromatic rice cultivars contain a badh2 gene producing a non-functional enzyme because of a premature stop codon. Such a truncated BADH2 enzyme can lead to the accumulation of 2AP, the main fragrant compound
additional information
several truncated or recombinant transcripts of BADH1 and BADH2 emerging from an unusual post-transcriptional process have been found in rice resulting in the insertion of exogenous gene sequences and different deletions leading to the elimination of the start codon, the loss of a functional domain and the introduction of a premature termination codon. Non-aromatic rice cultivars comprise a functional BADH2 gene, while aromatic rice cultivars contain a badh2 gene producing a non-functional enzyme because of a premature stop codon. Such a truncated BADH2 enzyme can lead to the accumulation of 2AP, the main fragrant compound
additional information
transgenic expression of the enzyme in Trachypsermum ammi to reduce salinity and drought stresses results in improved seedling fresh weight, plant height, proline content, relative water content, and secondary metabolites content. Recombinant expression in Nicotiana tabacum and Solanum lycopersicum to reduce temperature stress results in improved PSII efficiency, chlorophyll fluorescence, induction kinetics, activity of CAT, SOD and APX, and ascorbate and glutathione contents in tobacco, as well as in improved lipid peroxidation, glycine betaine accumulation, PSII photochemical activity, hydrogen peroxide and superoxide anion radical levels, CO2 assimilation, PSII photochemical activity, hydrogen peroxide, and superoxide anion radical and MDA levels in tomato. Recombinant expression in transgenic walnut plants to reduce drought and salinity stresses results in improved shoot height and survival rate
additional information
recombinant expression in trangenic Zea mays plants to reduce salinity and drought stresses results in improved glycine betaine (GB) accumulation, membrane permeability, and chlorophyll content, as well as altered morphological characteristics, GB accumulation, proline content, and levels of ROS, CAT, POX, SOD, and MDA
additional information
several truncated or recombinant transcripts of BADH1 and BADH2 emerging from an unusual post-transcriptional process have been found in rice resulting in the insertion of exogenous gene sequences and different deletions leading to the elimination of the start codon, the loss of a functional domain and the introduction of a premature termination codon. Such a truncated BADH2 enzyme can lead to the accumulation of 2AP, the main fragrant compound
additional information
transgenic expression of the enzyme in Arabidopsis thaliana to reduce salinity and drought stresses results in improved survival rate, fresh weight, relative water content, proline content, relative electrolyte leakage, MDA content root length, glycine betaine content, and RELs
additional information
Q53CF4
several truncated or recombinant transcripts of BADH1 and BADH2 emerging from an unusual post-transcriptional process have been found in rice resulting in the insertion of exogenous gene sequences and different deletions leading to the elimination of the start codon, the loss of a functional domain and the introduction of a premature termination codon. Such a truncated BADH2 enzyme can lead to the accumulation of 2AP, the main fragrant compound
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cloned in different strains (A764, A765, A767 and YPIC3) of Pichia pastoris
construction of a betaine aldehyde dehydrogenase/choline dehydrogenase fusion protein and expression in Escherichia coli and Nicotiana tabacum. Escherichia coli cells expressing the fusion protein are able to grow to higher final densities and to accumulate more glycine betaine than cells expressing choline dehydrogenase alone
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expressed in Arabidopsis thaliana
expressed in Escherichia coli
expressed in Escherichia coli BL21
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) Gold cells
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expressed in Escherichia coli BL21(DE3)/pMAGIC cells
expressed in Escherichia coli DH5alpha cells
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expressed in Escherichia coli Rosetta (DE3) cells
expressed in Escherichia coli strain BL21
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expressed in Ipomoea batatas cultivar Sushu-2 via Agrobacterium-mediated transformation
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expressed in Nicotiana tabacum
expressed in trifoliate orange Poncirus trifoliata by Agrobacterium-mediated transformation
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expression in Escherichia coli
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expression in Escherichia coli and Salmonella typhimurium
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expression in Escherichia coli cells
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expression in Nicotiana tabacum 89. Tobacco expressing BADH survives on Murashige-Skoog medium containing 200 mM NaCl, whereas the untransformed plants turn yellow after 20 d and die
For OsBADH2, preliminary experiments based on RT-PCR show that the mRNA is expressed constitutively and multiple transcription products ae detected. Primers specific to the 5' region are used. To analyze the transcripts derived from the OsBADH2 gene, seedlings from different varieties under different rowth conditions are harvested for the total RNA isolation. As a result, all the 59 cDNA clones sequenced also have deletions at the 5' exonic region. Similar to that in the OsBADH1 gene, various unusual events in the OsBADH2 locus generate a number of truncated transcripts. The size of the deleted sequences from 5' UTR and exon(s) range from 112 to 523 nucleotides.
gene AMADH1, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), quantitative real-time PCR enzyme expression analysis
gene BADH, Agrobacterium tumefaciens-mediated recombinant expression in Arabidopsis thaliana
gene BADH, Agrobacterium tumefaciens-mediated recombinant expression in Cichorium intybus and in Triticum aestivum
gene BADH, Agrobacterium tumefaciens-mediated recombinant expression in Solanum tuberosum and in Populus nigra
gene BADH, Agrobacterium tumefaciens-mediated recombinant expression in Trachyspermum ammi, Nicotiana tabacum, and Solanum lycopersicum, as well as in Juglans regia
gene BADH, BADH2 encodes on chromosome 8, sequence comparisons
gene BADH, microprojectile bombardment method-based transfection of Triticum aestivum
gene BADH, phylogenetic analysis, recombinant expression in Zea mays, quantitative RT-PCR expression analysis
gene BADH, recombinant expression in Zea mays via pollen-tube pathway
gene BADH, recombinant expression of AcBADH in transgenic Glycine max cv. Jinong 17 plants using the transfection method via Agrobacterium tumefaciens strain LBA4404, quntitative RT-PCR expression analysis
gene BADH, sequence comparisons
gene BADH, sequence comparisons, heterologous expression of a BADH gene from Ammopiptanthus nanus in Escherichia coli validates its role in abiotic tolerance
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gene BADH, sequence comparisons, recombinant expression of the enzyme in Escherichia coli strain ER2566
gene BADH1, DNA and amino acid sequence determination and analysis, recombinant enzyme expression in Escherichia coli strain M15 from vector pREP4 under the control of an inducible promoter
Halalkalibacterium halodurans
gene BADH1, sequence comparisons
gene BADH2, reconstructed from transcriptome, DNA and amino acid sequence determination and analysis, sequence comparisons, quantitative real-time PCR enzyme expression analysis
high-level expression of betaine aldehyde dehydrogenase in cultured cells, roots, and leaves of carrot via plastid genetic engineering. Homoplasmic transgenic plants that exhibit high levels of salt tolerance are regenerated from bombarded cell cultures via somatic embryogenesis. Transformation efficiency of carrot somatic embryos is very high, with one transgenic event per approximately seven bombarded plates under optimal conditions. In vitro transgenic carrot cells transformed with the badh transgene are visually green in color when compared to untransformed carrot cells, this offers a visual selection for transgenic lines. Transgenic carrot plants expressing BADH grow in presence of high concentrations of NaCl, up to 400 mM
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in Escherichia coli strain BL21 (DE3)
in Nicotiana tabacum, the BADH gene isolating from spinach is used to construct a vector plasmid that contained the promoter for 35S ribosomal RNA from CaMV35S, the sequence encoding the transit peptide of the small subunit of Rubisco of tobacco and the terminator of the gene for nopaline synthase. Nicotiana tabacum (wild type K326) is transformed with the resultant plasmid by the standard Agrobacterium-mediated method and five independent lines of transgenic tobacco plants are established. Transformed plants are used as the source of plant materials. The role of glycine betaine in vivo in protecting photosynthesis from salt stress is investigated.
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into the pCR2.1-TOPO and pGEX-6p-2 vector for sequencing of the coding region and expression of the enzyme in Escherichia coli BL21, respectively
into the pGEM-T easy vector for sequencing
mutant enzyme E103Q expressed in Escherichia coli
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of genes encoding five forms of spinach enzyme: full length, mature, mutant E103Q, mutant E103K and chimera
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overexpression in Escherichia coli
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partial characterization of the full-length BADH promoter of Suaeda liaotungensis through fusions of various lengths fused to the beta-glucuronidase coding sequence and subsequent expression in tobacco leaves treatment with NaCl are reported
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plasmid pCALbetB containing the full sequence of the gene betB that encodes PaBADH is used for the expression of the enzyme in Escherichia coli cells
Seeds from T2 generation (lines T2-1, T2-3, T2-5, T2-8 and T2-9) of transgenic tomato containing the BADH gene from Atriplex hortensis were used
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the BADH gene of Leymus chinensis is cloned by RT-PCR and RACE technology and is designated as LcBADH. The cDNA sequence of LcBADH is 1774 bp including the open reading frame of 1521 bp (coding 506 amino acids). The vector of prokaryotic expression is constructed by inserting the LcBADH gene fragment into pET30a(+) and transformed into Escherichia coli BL21(DE3)
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the gene betB, encoding for Pseudomonas aeruginosa betaine-aldehyde dehydrogenase, is cloned into a pCAL-n vector for sequencing and protein expression in Escherichia coli
To compare the posttranscriptional processing patterns of the BADH homologs between cereal crop species and more distantly related dicotyledonous species, RT-PCR experiments using total RNA extracted from seedlings of spinach are conducted. Primers designed to amplify the full length of mRNA of BADH homologs are used. As anticipated, the RT-PCR products of BADH homologs from Arabidopsis are of expected size for correctly processed transcripts. Sequencing analysis of 4 cDNA clones confirms the correct processing.
To compare the posttranscriptional processing patterns of the BADH homologs between cereal crop species and more distantly related dicotyledonous species, RT-PCR experiments using total RNA extracted from seedlings of spinach are conducted. Primers designed to amplify the full length of mRNA of BADH homologs are used. As anticipated, the RT-PCR products of BADH homologs from spinach are of expected size for correctly processed transcripts. Sequencing analysis of 4 cDNA clones confirms the correct processing.
To compare the posttranscriptional processing patterns of the BADH homologs between cereal crop species and more distantly related dicotyledonous species, RT-PCR experiments using total RNA extracted from seedlings of spinach are conducted. Primers designed to amplify the full length of mRNA of BADH homologs are used. As anticipated, the RT-PCR products of BADH homologs from tomato are of expected size for correctly processed transcripts. Sequencing analysis of 3 cDNA clones confirms the correct processing.
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To determine whether the unusual events occurring in the BADH transcripts are specific only to the rice genome, RT-PCR experiments using the total RNA extracted from seedlings of maize species are carried out. These experiments used primers either to amplify the full length of mRNA or exclusively the 5' region of BADH homologs corresponding to those in rice. The sequencing data from a total of 6 cDNA clones demonstrate that all the tested cDNA clones have deletion(s) of the 5' exonic sequences resulting from the unusual posttranscriptional processing.
Q53CF4
To determine whether the unusual events occurring in the transcripts are specific only to the rice genome, RT-PCR experiments using the total RNA extracted from seedlings of barley are performed. These experiments use primers either to amplify the full length of mRNA or exclusively the 5' region of BADH homologs corresponding to those in rice. The sequencing data from a total of 5 cDNA clones demonstrate that all the tested cDNA clones have deletions of the 5' exonic sequences resulting from the unusual posttranscriptional processing.
To determine whether the unusual events occurring in the transcripts are specific only to the rice genome, RT-PCR experiments using the total RNA extracted from seedlings of maize are performed. These experiments use primers either to amplify the full length of mRNA or exclusively the 5' region of BADH homologs corresponding to those in rice. The sequencing data from a total of 9 cDNA clones demonstrate that all the tested cDNA clones have deletions of the 5' exonic sequences resulting from the unusual posttranscriptional processing.
Q53CF4
To determine whether the unusual events occurring in the transcripts are specific only to the rice genome, RT-PCR experiments using the total RNA extracted from seedlings of wheat are performed. These experiments use primers either to amplify the full length of mRNA or exclusively the 5' region of BADH homologs corresponding to those in rice. Sequencing data from 22 DNA clones demonstrate that all the tested cDNA clones had deletion(s) of the 5' exonic sequences resulting from the unusual posttranscriptional processing.
To determine whether the unusual events occurring in the transcripts are specific only to the rice genome, RT-PCR experiments using the total RNA extracted from seedlings wheat are performed. These experiments use primers either to amplify the full length of mRNA or exclusively the 5' region of BADH homologs corresponding to those in rice. Sequencing data from 4 DNA clones demonstrate that all the tested cDNA clones had deletion(s) of the 5' exonic sequences resulting from the unusual posttranscriptional processing.
To determine whether the unusual events occurring in the transcripts were specific only to the rice genome, RT-PCR experiments using the total RNA extracted from seedlings of barley are performed. These experiments use primers either to amplify the full length of mRNA or exclusively the 5' region of BADH homologs corresponding to those in rice. The sequencing data from a total of 6 cDNA clones demonstrate that all the tested cDNA clones have deletions of the 5' exonic sequences resulting from the unusual posttranscriptional processing.
to examine whether the expressed products are OsBADh1 gene, the RT-PCR-amplified fragments are cloned and sequenced. Primers derived from 5' and 3' untranslated regions are used to isolate the full length of OsBADH1 cDNA clones. Resultant sequencing analysis reveal that the cDNAs are truncated at the 5' exonic region. Observed expression products are shorter than the expected size of 695 bp of the 5' exonic region. Sequence comparison of the cDNAs reveal a considerable variation in their structural compositions. All of the cDNAs contain a deletion of the 5' coding sequence within the OsBADH1 gene. The deleted exon material ranged from 28 to 225 nucleotides in size. The start-point of the deletions in four cDNAs begin with the first nucleotide of the coding sequence, which give rise to the loss of translation initiation codon. 32 cDNAs encode derivatives with frame-shifts in the open reading frame , introducing various stop codons at different positions. Only 5 cDNA clones show the potential to encode partial BADH1 proteins with deletions that code for a part of the putative NAD+ binding domain. Most of the missing sequences from the truncated transcripts indicate above involved 2 different exons, and in a few cases the truncation take place within a single exon. In addition, two independent deletions of exon materials within a single cDNA clone are observed in 5 clones. Therefore, no cDNA is found to have the capacity to encode the full length of the OsBADH1 protein, indicating that correctly processed transcripts represent a very small proportion of the total cytoplasmic mature OsBADH1 RNA population and consequently that the majority of the OsBADH1 mRNAs are unlikely to encode functional proteins.
wild type Pseudomonas aeruginosa betaine aldehyde dehydrogenase and the four mutants C353A, C377A, C439A and C286A
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expressed in Escherichia coli
expressed in Escherichia coli
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expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
gene BADH, Agrobacterium tumefaciens-mediated recombinant expression in Arabidopsis thaliana
gene BADH, Agrobacterium tumefaciens-mediated recombinant expression in Arabidopsis thaliana
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gene BADH, sequence comparisons
Q53CF4
gene BADH, sequence comparisons
gene BADH, sequence comparisons
gene BADH, sequence comparisons
gene BADH, sequence comparisons
gene BADH, sequence comparisons
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.