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Information on EC 1.2.1.8 - betaine-aldehyde dehydrogenase
for references in articles please use BRENDA:EC1.2.1.8
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EC Tree 1 Oxidoreductases
1.2 Acting on the aldehyde or oxo group of donors
1.2.1 With NAD+ or NADP+ as acceptor
1.2.1.8 betaine-aldehyde dehydrogenase
IUBMB Comments
In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria. In contrast, different enzymes are involved in the first reaction. In plants, this reaction is catalysed by EC 1.14.15.7 (choline monooxygenase), whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase) . In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase).
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.2.1.8
-
badhs
- aroma
-
fragrant
-
2-acetyl-1-pyrroline
-
osmoprotectant
- molecular biology
-
basmati
-
non-fragrant
-
scent
- 4-aminobutyraldehyde
- medicine
- 3-aminopropionaldehyde
-
non-aromatic
- aminoaldehyde
-
jasmine
- agriculture
- biotechnology
- energy production
- food industry
showSynonyms
badh2, badh1, pabadh, osbadh2, betaine-aldehyde dehydrogenase, betaine aldehyde dehydrogenase 2, osbadh1, pkbadh, badh2-e7, badh2-e2, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AcBADH
ATRR
BADH
BADH1
BADH2
badh2-E2
recessive allele, truncated form, with a 7-bp deletion in exon 2 (82 residues)
betaine aldehyde dehydrogenase
betaine aldehyde dehydrogenase 2
betaine aldehyde oxidase
-
-
-
-
betaine aldehyde: NAD(P)+ oxidoreductase
betaine aldehyde:NAD(P)+ oxidoreductase
BetB
dehydrogenase, betaine aldehyde
-
-
-
-
glycine betaine reductase
PaBADH
pkBADH
ZBD1
-
Zoysia betaine aldehyde dehydrogenase 1
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BADH
-
-
-
-
BADH
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betaine aldehyde dehydrogenase
-
-
-
-
betaine aldehyde dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
steady-state ordered bi bi or rapid equilibrium mechanism
-
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
ping-pong mechanism
-
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
iso-ordered bi-bi steady state mechanism
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betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
iso-ordered bi-bi steady state mechanism
-
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
iso random steady state mechanism
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betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
NAD+ is the first substrate to bind to the enzyme and NADH is the last product to dissociate from it
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betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
steady-state ordered mechanism, in which NAD+ binds first and NADH leaves last
-
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
the enzyme catalyzes the second step of the two-step conversion of choline into glycine betaine
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
catalyzes the last irreversible step in the synthesis of the osmoprotector glycine betaine
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betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
catalyzes the last step of the two-step oxidation
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betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
porcine kidney BADH follows an iso bi-bi ordered mechanism in which NAD+ is the first substrate to bind to pkBADH and NADH is the last product released
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betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
ping-pong mechanism
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betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
reduction
oxidation
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oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
beta-alanine biosynthesis I, beta-alanine biosynthesis IV, choline degradation I, choline degradation IV, dimethylsulfoniopropanoate biosynthesis I (Wollastonia), dimethylsulfoniopropanoate biosynthesis II (Spartina), glycine betaine biosynthesis I (Gram-negative bacteria), glycine betaine biosynthesis II (Gram-positive bacteria), glycine betaine biosynthesis III (plants)
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SYSTEMATIC NAME
IUBMB Comments
betaine-aldehyde:NAD+ oxidoreductase
In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria. In contrast, different enzymes are involved in the first reaction. In plants, this reaction is catalysed by EC 1.14.15.7 (choline monooxygenase), whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase) [5]. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase).
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CAS REGISTRY NUMBER
COMMENTARY
9028-90-4
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-aminopropionaldehyde + NAD(P)+ + H2O
?
Substrates: -
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?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropanoate + NADH + H+
-
Substrates: -
Products: -
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?
3-dimethylsulfoniopropionaldehyde + NAD(P)+ + H2O
?
Substrates: -
Products: -
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?
3-dimethylsulfoniopropionaldehyde + NAD+ + O2
3-dimethylsulfoniopropionate + NADH
-
Substrates: steady state bi bi mechanism with ordered addition of substrates and random release of products
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3-N-trimethylaminopropionaldehyde + NAD+ + H2O
3-N-trimethylaminopropanoate + NADH + H+
-
Substrates: -
Products: -
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?
3-N-trimethylaminopropionaldehyde + NAD+ + H2O
3-N-trimethylaminopropionate + NADH + H+
-
Substrates: -
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?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH
-
Substrates: -
Products: -
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?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
Substrates: -
Products: -
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?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH + 2 H+
Substrates: -
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?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH + H+
Substrates: -
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?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutyrate + NADH + H+
-
Substrates: -
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?
4-N-trimethylaminobutyraldehyde + NAD(P)+ + H2O
?
Substrates: -
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?
4-N-trimethylaminobutyraldehyde + NAD+ + H2O
4-N-trimethylaminobutyrate + NADH + H+
-
Substrates: -
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?
4-N-trimethylaminobutyraldehyde + NAD+ + H2O
4-N-trmethylaminobutanoate + NADH + H+
-
Substrates: -
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?
4-trimethylaminobutyraldehyde + NAD+ + H2O
3-trimethylaminobutyrate + NADH
-
Substrates: -
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?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
Substrates: -
Products: -
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?
aminoacetaldehyde + NAD+ + H2O
aminoacetate + NADH + H+
-
Substrates: -
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?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
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?
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
-
Substrates: -
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?
betaine aldehyde + NAD(P)+ + H2O
betaine + NAD(P)H + H+
Substrates: -
Products: -
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?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + 2 H+
-
Substrates: -
Products: -
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ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + 2 H+
Substrates: -
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r
betaine aldehyde + NADP+ + H2O
glycine betaine + NADPH + H+
Substrates: -
Products: -
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ir
butyraldehyde + NAD+ + H2O
butyrate + NADH
-
Substrates: at 40% of the activity with betaine aldehyde
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butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
-
Substrates: -
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butyraldehyde + NADP+ + H2O
butyrate + NADPH + H+
-
Substrates: -
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?
DL-glyceraldehyde + NAD+ + H2O
glycerate + NADH + H+
-
Substrates: -
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?
DL-glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
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Substrates: -
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?
formaldehyde + NADP+ + H2O
formate + NADPH + H+
-
Substrates: -
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?
gamma-aminobutyraldehyde + NAD(P)+ + H2O
?
Substrates: -
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?
glyceraldehyde + NAD+ + H2O
glycerate + NADH
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Substrates: at 30% of the activity with betaine aldehyde
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?
glycine betaine aldehyde + NAD+ + H2O
glycine betaine + NADH
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Substrates: -
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glycine betaine aldehyde + NADP+ + H2O
glycine betaine + NADPH
-
Substrates: -
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glycolaldehyde + NAD+ + H2O
glycolate + NADH + H+
-
Substrates: -
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glycolaldehyde + NADP+ + H2O
glycolate + NADPH + H+
-
Substrates: -
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?
isovaleraldehyde + NAD+ + H2O
isovalerate + NADH + H+
-
Substrates: -
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?
isovaleraldehyde + NADP+ + H2O
isovalerate + NADPH + H+
-
Substrates: -
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methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
Substrates: -
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?
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoate + NADH + H+
-
Substrates: -
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?
p-nitrobenzaldehyde + NADP+ + H2O
p-nitrobenzoate + NADPH + H+
-
Substrates: -
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?
phenyl acetaldehyde + NAD+ + H2O
phenyl acetate + NADH + H+
-
Substrates: -
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?
phenyl acetaldehyde + NADP+ + H2O
phenyl acetate + NADPH + H+
-
Substrates: -
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?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
Substrates: -
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propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
-
Substrates: -
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undecanal + NAD+ + H2O
undecanoate + NADH + H+
-
Substrates: -
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undecanal + NADP+ + H2O
undecanoate + NADPH + H+
-
Substrates: -
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valeraldehyde + NAD+ + H2O
valerate + NADH + H+
-
Substrates: -
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valeraldehyde + NADP+ + H2O
valerate + NADPH + H+
-
Substrates: -
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3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
Substrates: -
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?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
-
Substrates: -
Products: -
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?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
Substrates: -
Products: -
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?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionic acid + NADH + H+
-
Substrates: -
Products: -
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?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionic acid + NADH + H+
Substrates: -
Products: -
Products: -
?
3-N-trimethylaminopropionaldehyde + NAD+ + H2O
?
-
Substrates: -
Products: -
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?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
-
Substrates: -
Products: -
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?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
-
Substrates: -
Products: -
Products: -
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
-
Substrates: no activity
Products: -
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?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
-
Substrates: -
Products: -
Products: -
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
-
Substrates: -
Products: -
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?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
Substrates: -
Products: -
Products: -
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
-
Substrates: -
Products: -
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?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
Substrates: -
Products: -
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?
4-N-trimethylaminobutyraldehyde + NAD+ + H2O
?
-
Substrates: -
Products: -
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?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
Substrates: at 20% of the activity with betaine aldehyde
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?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
-
Substrates: -
Products: -
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?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
Substrates: -
Products: -
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ir
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
-
Substrates: -
Products: -
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?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
Substrates: -
Products: -
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ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: synthesis of betaine
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
Products: -
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ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: enzyme catalyzes the final irreversible step in the synthesis of glycine betaine
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: the enzyme is involved in the metabolism of choline, induced during growth on choline
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: the enzyme is involved in the metabolism of choline, induced during growth on choline
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: synthesis of betaine
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: synthesis of betaine
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: synthesis of betaine
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: highly specific for betaine aldehyde
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: enzyme of the osmoregulatory choline-glycine betaine pathway
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: the salt tolerance is an essential property for the enzyme participating in the cellular synthesis of an osmoprotectant
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: synthesis of betaine
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: synthesis of betaine
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: synthesis of betaine
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: reverse reaction not detected
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: preferentially uses NADP+ over NAD+
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: 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
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: inducible enzyme accumulates in the presence of choline, acetylcholine or betaine in the medium
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: reverse reaction not detected
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: inducible enzyme accumulates in the presence of choline, acetylcholine or betaine in the medium
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: 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
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: the age-related acceleration in conversion of choline into betaine probably tends to diminish unesterified choline concentrations
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: enzyme is induced several-fold by salinization
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: synthesis of betaine
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: equilibrium of the reaction strongly favours betaine formation
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: enzyme is induced several-fold by salinization
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: synthesis of betaine
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: last step in betaine synthesis, a nontoxic or protective osmolyte under saline or dry conditions
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
Substrates: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
Substrates: -
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Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
Substrates: -
Products: accumulation of betaine is a strategy of plants to survive drought, salinity, and extreme temperatures
Products: accumulation of betaine is a strategy of plants to survive drought, salinity, and extreme temperatures
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Vallaris sp.
-
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Q53CF4
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
Substrates: -
Products: regulates osmotic pressure and protects enzyme activities; the transgenic plants have a higher accumulation of betaine
Products: regulates osmotic pressure and protects enzyme activities; the transgenic plants have a higher accumulation of betaine
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betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
Substrates: the enzyme catalyzes the second step in the synthesis of the osmoprotectant glycine betaine
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
Substrates: 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
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
Substrates: more active on medium-chain aldehydes than on betaine aldehyde
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
Substrates: belongs to the NAD-dependent dehydrogenase family, characterized by the typical aldehyde substrate binding domain
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
Substrates: -
Products: -
Products: -
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
Substrates: -
Products: 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
Products: 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+
Substrates: -
Products: 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.
Products: 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+
-
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
Substrates: -
Products: glycine betaine is not only an nontoxic osmoprotectant but also maintains protein and membrane conformations under various stress conditions
Products: 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+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
Substrates: -
Products: 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
Products: 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+
Substrates: -
Products: 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
Products: 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+
-
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
Substrates: -
Products: -
Products: -
ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
Substrates: -
Products: 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.
Products: 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.
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betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
Substrates: -
Products: 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
Products: 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
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betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
Substrates: glycine betaine synthesis; two-step oxidation involving choline monooxygenase and BADH
Products: recombinant yeasts transformed with the two genes CMO and BADH exhibited higher tolerance to salt, methanol and high temperature stress.
Products: recombinant yeasts transformed with the two genes CMO and BADH exhibited higher tolerance to salt, methanol and high temperature stress.
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betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
Substrates: -
Products: -
Products: -
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betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
Substrates: -
Products: -
Products: -
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betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
Substrates: -
Products: -
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betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
Substrates: NAD+ is preferred over NADP+
Products: -
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betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
Substrates: -
Products: -
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betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
Substrates: preferentially uses NADP+ over NAD+
Products: -
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betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
Substrates: no activity with NAD+
Products: -
Products: -
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betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
Substrates: -
Products: -
Products: -
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betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
Substrates: no activity with NAD+
Products: -
Products: -
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betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
Substrates: 75% of the activity with NAD+
Products: -
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betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
Substrates: 25% of the maximal activity with NAD+
Products: -
Products: -
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betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
Substrates: -
Products: -
Products: -
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betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
-
Substrates: more active on medium-chain aldehydes than on betaine aldehyde
Products: -
Products: -
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betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
-
Substrates: low activity with NADP+
Products: -
Products: -
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betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
-
Substrates: 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
Products: -
Products: -
ir
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
-
Substrates: -
Products: -
Products: -
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betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
Substrates: -
Products: -
Products: -
ir
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
Substrates: the enzyme is also active with NADP+, but the NAD-supported activity is at least 10times higher
Products: -
Products: -
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glycine betaine + NADPH + H+
glycine betaine aldehyde + NADP+
Substrates: -
Products: -
Products: -
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glycine betaine + NADPH + H+
glycine betaine aldehyde + NADP+
Substrates: -
Products: -
Products: -
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glycolaldehyde + NAD+ + H2O
glycolate + NADH
-
Substrates: -
Products: -
Products: -
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N,N-dimethylglycine + NADPH + H+
?
Substrates: about 70% activity compared to glycine betaine
Products: -
Products: -
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N,N-dimethylglycine + NADPH + H+
?
Substrates: about 70% activity compared to glycine betaine
Products: -
Products: -
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additional information
?
-
Substrates: no activity with L-carnithine, butyrobetaine, beta-alanine betaine, stachydrine, hercynine, ergothionine, sarcosine, 3,3-dimethylbutyrate, and proteinogenic amino acids
Products: -
Products: -
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additional information
?
-
Substrates: no activity with L-carnithine, butyrobetaine, beta-alanine betaine, stachydrine, hercynine, ergothionine, sarcosine, 3,3-dimethylbutyrate, and proteinogenic amino acids
Products: -
Products: -
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additional information
?
-
-
Substrates: no activity with succinic semialdehyde
Products: -
Products: -
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additional information
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-
Substrates: 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)
Products: -
Products: -
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additional information
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-
Halalkalibacterium halodurans SMBPL06
Substrates: 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)
Products: -
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additional information
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-
Substrates: the enzyme is also active with 4-aminobutyraldehyde and 3-aminopropionaldehyde, EC 1.2.1.19
Products: -
Products: -
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additional information
?
-
Substrates: 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.
Products: -
Products: -
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additional information
?
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Substrates: 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.
Products: -
Products: -
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additional information
?
-
Substrates: 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.
Products: -
Products: -
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additional information
?
-
-
Substrates: 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.
Products: -
Products: -
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additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
Products: -
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additional information
?
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: various other C3-C6 amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: isozyme BADH1 catalyzes the oxidation of acetaldehyde efficiently, while the activity of isozyme BADH2 is extremely low
Products: -
Products: -
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additional information
?
-
Substrates: 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
Products: -
Products: -
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additional information
?
-
Substrates: 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
Products: -
Products: -
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additional information
?
-
Substrates: 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
Products: -
Products: -
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additional information
?
-
Substrates: 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
Products: -
Products: -
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additional information
?
-
Substrates: betaine aldehyde substrates docking study, overview. The enzyme shows a good affinity with both betaine aldehyde (BAD) and 4-aminobutyraldehyde (GABald) as substrates
Products: -
Products: -
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additional information
?
-
-
Substrates: betaine aldehyde substrates docking study, overview. The enzyme shows a good affinity with both betaine aldehyde (BAD) and 4-aminobutyraldehyde (GABald) as substrates
Products: -
Products: -
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additional information
?
-
-
Substrates: no activity with 3-dimethylsulfoniopropionaldehyde
Products: -
Products: -
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additional information
?
-
Substrates: 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
Products: -
Products: -
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additional information
?
-
-
Substrates: 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
Products: -
Products: -
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additional information
?
-
-
Substrates: betaine aldehyde dehydrogenase gene expression in leaves increases with salt stress
Products: -
Products: -
?
additional information
?
-
-
Substrates: betaine aldehyde dehydrogenase gene expression in leaves increases with salt stress
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH + H+
Substrates: -
Products: -
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?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + 2 H+
-
Substrates: -
Products: -
Products: -
ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
r
betaine aldehyde + NADP+ + H2O
glycine betaine + NADPH + H+
Substrates: -
Products: -
Products: -
ir
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
Substrates: -
Products: -
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?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
Substrates: -
Products: -
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?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
Substrates: -
Products: -
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?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
-
Substrates: -
Products: -
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?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
-
Substrates: -
Products: -
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?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
Substrates: -
Products: -
Products: -
ir
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
Substrates: -
Products: -
Products: -
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: synthesis of betaine
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: enzyme catalyzes the final irreversible step in the synthesis of glycine betaine
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: the enzyme is involved in the metabolism of choline, induced during growth on choline
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: the enzyme is involved in the metabolism of choline, induced during growth on choline
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: synthesis of betaine
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: synthesis of betaine
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: synthesis of betaine
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: enzyme of the osmoregulatory choline-glycine betaine pathway
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: the salt tolerance is an essential property for the enzyme participating in the cellular synthesis of an osmoprotectant
Products: -
Products: -
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: synthesis of betaine
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: -
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: synthesis of betaine
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: synthesis of betaine
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: 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
Products: -
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ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: inducible enzyme accumulates in the presence of choline, acetylcholine or betaine in the medium
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: inducible enzyme accumulates in the presence of choline, acetylcholine or betaine in the medium
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: 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
Products: -
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betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: the age-related acceleration in conversion of choline into betaine probably tends to diminish unesterified choline concentrations
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: enzyme is induced several-fold by salinization
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: synthesis of betaine
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: enzyme is induced several-fold by salinization
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: synthesis of betaine
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
Substrates: last step in betaine synthesis, a nontoxic or protective osmolyte under saline or dry conditions
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
Substrates: -
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
Substrates: -
Products: accumulation of betaine is a strategy of plants to survive drought, salinity, and extreme temperatures
Products: accumulation of betaine is a strategy of plants to survive drought, salinity, and extreme temperatures
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Vallaris sp.
-
Substrates: -
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
Q53CF4
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
Substrates: -
Products: regulates osmotic pressure and protects enzyme activities; the transgenic plants have a higher accumulation of betaine
Products: regulates osmotic pressure and protects enzyme activities; the transgenic plants have a higher accumulation of betaine
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
Substrates: the enzyme catalyzes the second step in the synthesis of the osmoprotectant glycine betaine
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
Substrates: -
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
Substrates: 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
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betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
Substrates: -
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
Substrates: belongs to the NAD-dependent dehydrogenase family, characterized by the typical aldehyde substrate binding domain
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
Substrates: -
Products: -
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?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
Substrates: -
Products: -
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?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
Substrates: -
Products: 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
Products: 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+
Substrates: -
Products: 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.
Products: 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+
-
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
Substrates: -
Products: glycine betaine is not only an nontoxic osmoprotectant but also maintains protein and membrane conformations under various stress conditions
Products: 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+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
Substrates: -
Products: 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
Products: 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+
Substrates: -
Products: 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
Products: 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+
-
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
Substrates: -
Products: -
Products: -
ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
Substrates: -
Products: 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.
Products: 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+
-
Substrates: -
Products: 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
Products: 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+
Substrates: glycine betaine synthesis; two-step oxidation involving choline monooxygenase and BADH
Products: recombinant yeasts transformed with the two genes CMO and BADH exhibited higher tolerance to salt, methanol and high temperature stress.
Products: 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+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
Substrates: -
Products: -
Products: -
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: 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.
Products: -
Products: -
?
additional information
?
-
Substrates: 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.
Products: -
Products: -
?
additional information
?
-
Substrates: 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.
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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.
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
Products: -
?
additional information
?
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Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: betaine aldehyde dehydrogenase gene expression in leaves increases with salt stress
Products: -
Products: -
?
additional information
?
-
-
Substrates: betaine aldehyde dehydrogenase gene expression in leaves increases with salt stress
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
NAD+
The BADH2 enzyme is predicted to contain three domains: NAD binding, substrate binding, and oligomerization domain
NAD+
the enzyme is also active with NADP+, but the NAD-supported activity is at least 10times higher
NAD+
-
the enzyme can use both NAD+ and NADP+ as cofactors, but the NAD+-dependent activity is at least 10 times higher
NAD+
-
porcine kidney betaine aldehyde dehydrogenase (pkBADH) binds NAD+ with different affinities at each active site and the binding is K+ dependent
NAD+
pkBADH/NAD+ interaction analysis by circular dichroism (CD) and by isothermal titration calorimetry (ITC) by titrating the enzyme with NAD+
NADP+
the enzyme is also active with NADP+, but the NAD-supported activity is at least 10times higher
NADP+
-
the enzyme can use both NAD+ and NADP+ as cofactors, but the NAD+-dependent activity is at least 10 times higher
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cl-
K+
Mg2+
Na+
NH4+
additional information
-
high salt tolerance: 50% or more of its maximal activity is preserved at 1.0 M Na+ or K+
Ca2+
-
results indicate that transgenic plants have a higher Ca2+ accumulation than the wild type under saline conditions
Ca2+
-
increase of concentration from 0 to 0.00075 mM produces a 2fold increase in activity
Cl-
-
results indicate that transgenic plants have a lower Cl- accumulation than the wild type under saline conditions
Cl-
BADH plays an important role in the tolerance of plants to salinity
K+
-
results indicate that transgenic plants have a higher K+ accumulation than the wild type under saline conditions
K+
-
required for maintenance of its active conformation. At low concentrations, the enzyme is totally inactivated upon removal of K+. NAD+ protects against inactivation by absence of K+, betaine aldehyde affords partial protection. NH4+ but not Na+ can mimic the effect of K+. At pH 7.0 in the absence of K+ in a buffer of low ionic strength, the active tetrameric form dissociates into inactive monomers
K+
the enzyme requires K+ ions for stability and possesses two K+ binding sites per subunit
K+
-
required for maintenance of its active conformation. At low concentrations, the enzyme is totally inactivated upon removal of K+. NAD+ protects against inactivation by absence of K+, betaine aldehyde incrrases the inactivation rate of the enzyme. NH4+ but not Na+ can mimic the effect of K+. At pH 7.0 in the absence of K+ in a buffer of low ionic strength, the active tetrameric form dissociates into inactive monomers
K+
-
required for binding of cofactor NAD+. K+ causes small changes in secondary and tertiary structures that influences the active site conformation, binding of K+ to the enzyme caused changes in the alpha-helix content of 4% and 12% in the presence of 25 mM and 100 mM K+, respectively
K+
presence of K+ stabilizes the enzyme secondary structure and maintains its alpha-helix content. K+ increases the thermal stability of the pkBADHNAD+ complex by 5.3°C
Na+
-
results indicate that transgenic plants have a lower Na+ accumulation than the wild type under saline conditions
Na+
BADH plays an important role in the tolerance of plants to salinity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
-
mutant enzyme is less sensitive to inhibition than wild-type enzyme
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
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
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
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
Isovaleraldehyde
-
wild-type enzyme shows stronger inhibition than the mutant enzyme
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
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-methylmethanesulfonate
-
the effect of the thiol reagent MMTS on the native enzyme structure of the wild type enzyme and the mutants is examined
tetramethylammonium ion
the enzyme is not potently inhibited by the head-group mimic tetramethylammonium ion
AMP
-
competitive with respect to NAD+ and mixed with betaine aldehyde and uncompetitive with respect to NAD+
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
choline
mixed-type inhibitor for both glycine betaine reductase and aldehyde reductase activity
choline
-
mutant enzyme shows stronger inhibition compared to wild-type enzyme
choline
-
competitive against betaine aldehyde and uncompetitive with respect to NAD+
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.
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
-
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
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
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
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
methanol
used in the assay as activating compound in concentration of 0.5% for 96 h
propan-2-yl 1-thio-beta-D-galactopyranoside
-
for the expressed protein, final concentration of 1 mmol in culture solution
NaCl
-
enzyme activity and betaine content are almost undetectable in the wild type under either normal or stressed conditions. The transgenic plants exhibit low levels of BADH activity under normal conditions, while the enzyme activity increases up to 20-fold when stressed by 1.0% and 1.5% NaCl.
NaCl
Expression of JcBD1 protein under different salt concentrations increased clearly in recombinant plasmid transgenic cells at the presence of 100-400 mM NaCl
NaCl
expression of OsBADH1 gene was very low without salt stress and increased under salt stress conditions. However, a high ion concentration (0.5 M) inhibited trancription of this gene
NaCl
expression of OsBADH2 gene is low without salt stress and increased under salt stress conditions. A high ion concentration (0.5 M) inhibited trancription of the gene
NaCl
-
with an increase in environmental NaCl concentration, the level of BADH transcription and expression rises by activation of the promotor region
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Disulfiram irreversibly aggregates betaine aldehyde dehydrogenase--a potential target for antimicrobial agents against Pseudomonas aeruginosa.
Infections
The disulfiram metabolites S-methyl-N,N-diethyldithiocarbamoyl sulfoxide and S-methyl-N,N-diethylthiocarbamoyl sulfone irreversibly inactivate betaine aldehyde dehydrogenase from Pseudomonas aeruginosa, both in vitro and in situ, and arrest bacterial growth.
Starvation
Upregulation of stress response genes and ABC transporters in anaerobic stationary-phase Mycobacterium smegmatis.
Tuberculosis
Upregulation of stress response genes and ABC transporters in anaerobic stationary-phase Mycobacterium smegmatis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
0.34
3-N-trimethylaminopropionaldehyde
-
isozyme BADH2, pH and temperature not specified in the publication
0.049
4-Aminobutyraldehyde
-
1.1
4-Aminobutyraldehyde
in 100 mM sodium diphosphate pH 8.0, at 22°C
0.0078
4-N-trimethylaminobutyraldehyde
-
isozyme BADH1, pH and temperature not specified in the publication
0.041
4-N-trimethylaminobutyraldehyde
-
isozyme BADH2, pH and temperature not specified in the publication
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
0.15
Betaine aldehyde
-
pH 7.5, 20°C, native betaine-aldehyde dehydrogenase or betaine aldehyde dehydrogenase/choline dehydrogenase fusion protein
0.23
Betaine aldehyde
-
isozyme BADH2, pH and temperature not specified in the publication
0.291
Betaine aldehyde
-
0.665
Betaine aldehyde
pH 8.0, 30°C, recombinant isozyme LrAMADH1
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
6.81
Betaine aldehyde
in 100 mM sodium diphosphate pH 8.0, at 22°C
2.2
glycine betaine
mutant enzyme G1036A/Y1178F, at pH 7.5 and 30°C
0.24
glycine betaine aldehyde
wild type enzyme, at pH 7.5 and 30°C
0.24
glycine betaine aldehyde
mutant enzyme Y811F, at pH 7.5 and 30°C
1.5
glycine betaine aldehyde
mutant enzyme Y1178F, at pH 7.5 and 30°C
2.6
glycine betaine aldehyde
mutant enzyme G1036A/Y1178F, at pH 7.5 and 30°C
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
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.023
N,N-dimethylglycine
wild type enzyme, at pH 7.5 and 30°C
0.004
Betaine aldehyde
pH 8.0, 30°C, recombinant isozyme LrAMADH1
1.8
Betaine aldehyde
-
mutant enzyme H448F/P449M/Y450L, at pH 8.0 and 30°C
0.66
glycine betaine
mutant enzyme G1036A/Y1178F, at pH 7.5 and 30°C
0.72
glycine betaine
mutant enzyme Y1178F, at pH 7.5 and 30°C
0.018
glycine betaine aldehyde
mutant enzyme G1036A/Y1178F, at pH 7.5 and 30°C
0.3
glycine betaine aldehyde
mutant enzyme Y1178F, at pH 7.5 and 30°C
7
glycine betaine aldehyde
mutant enzyme Y811F, at pH 7.5 and 30°C
7.1
glycine betaine aldehyde
wild type enzyme, at pH 7.5 and 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.004
N,N-dimethylglycine
wild type enzyme, at pH 7.5 and 30°C
0.006
Betaine aldehyde
pH 8.0, 30°C, recombinant isozyme LrAMADH1
0.39
Betaine aldehyde
-
mutant enzyme H448F/P449M/Y450L, at pH 8.0 and 30°C
0.3
glycine betaine
mutant enzyme G1036A/Y1178F, at pH 7.5 and 30°C
0.33
glycine betaine
mutant enzyme Y1178F, at pH 7.5 and 30°C
0.007
glycine betaine aldehyde
mutant enzyme G1036A/Y1178F, at pH 7.5 and 30°C
0.19
glycine betaine aldehyde
mutant enzyme Y1178F, at pH 7.5 and 30°C
29
glycine betaine aldehyde
mutant enzyme Y811F, at pH 7.5 and 30°C
30
glycine betaine aldehyde
wild type enzyme, at pH 7.5 and 30°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5
tetramethylammonium ion
wild type enzyme, at pH 7.5 and 30°C
0.34
Betaine aldehyde
-
pH and temperature not specified in the publication
0.27
choline
wild type enzyme, competing against glycine betaine, at pH 7.5 and 30°C
6.7
choline
wild type enzyme, competing against glycine betaine aldehyde, at pH 7.5 and 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00826
0.012
culture conditions, 11.1 mM glucose, 15 mM NH4Cl and 0.4 M NaCl
0.211
culture conditions, 11.1 mM glucose, 20 mM choline and 0.4 M NaCl
19.63
cloned in strain A764 and extracted, incubating at 30°C for 96 h in presence of 0.5% of methanol. Activity was measured spectrophotometrically at 340 nm in 1 ml assay buffer (50 mmol HEPES-KOH (pH 8.0), 1 mmol EDTA, 5 mmol DTT, 1 mmol NAD+, 1 mmol betaine aldehyde) at 25°C, supplemented with 50 microliter protein extract. Activity is calculated using an extinction coefficient of 6.220 M/cm for NADH. One unit of enzyme activity is defined as the amount converting 1 nmol of NAD+ per min
additional information
0.00826
-
specific activity of expressed protein after 3 h IPTG induction. After disruption of the cells by ultrasonication, supernatant is used to assay the enzyme activity. Reaction is started by adding 0.05 ml of 10 mmol/l betaine aldehyde chloride at 30°C and lasted for 30 min. Specific activity is detected in crude enzyme extracts. BADH activity from induced bacteria is 75.3% higher than in the control.
additional information
activities assayed in 400 ml of reaction mixture consisting of 20 mM TrisHCl buffer, 0.5 mM NAD+, 5 mM DTT, and 100 ml purified protein elutes solution or crude bacterial extracts. The substrate betaine aldehyde is added to the reaction mixtures after preincubation for 10 min at 37°C to start the reactions. Enzyme activities are determined according to the absorbance at 340 nm (reflecting the consumption of NAD+). One unit of the activity is defined as 1 micromol/min of NAD+ consumption. The purified recombinant protein solution and crude bacterial extracts of the transformed cells both show high enzymatic activities. The activity is 2.53 nmol/ml and 2.06 nmol/ml, respectively, whereas crude bacterial extracts of untransformed Escherichia coli is 0.68 nmol/ml
additional information
Determination of aldehyde dehydrogenase activity of purified intact BADH2 and partial BADH2 using various aldehyde substrates (1 mM betaine aldehyde, 50 microM 4-aminobutyraldehyde, and 50 microM 3-aminopropionaldehyde). Enzymatic activities were spectrophotometrically assayed by A340 at pH 8.0 at intervals of 0, 10, 20, 30, and 60 min after the initiation of reactions. The intact BADH2 showed high betaine aldehyde dehydrogenase activity, with a rapid increase in A340 within the first 10 min after the enzymatic reaction. In addition, intact BADH2 also showed strong 4-aminobutyraldehyde and 3-aminopropionaldehyde dehydrogenase activities.
additional information
Determination of aldehyde dehydrogenase activity of purified intact BADH2 and partial BADH2 using various aldehyde substrates (1 mM betaine aldehyde, 50 microM 4-aminobutyraldehyde, and 50 microM 3-aminopropionaldehyde). Enzymatic activities were spectrophotometrically assayed by A340 at pH 8.0 at intervals of 0, 10, 20, 30, and 60 min after the initiation of reactions. The intact BADH2 showed high betaine aldehyde dehydrogenase activity, with a rapid increase in A340 within the first 10 min after the enzymatic reaction. In addition, intact BADH2 also showed strong 4-aminobutyraldehyde and 3-aminopropionaldehyde dehydrogenase activities.
additional information
Determination of aldehyde dehydrogenase activity of purified intact BADH2 and partial BADH2 using various aldehyde substrates (1 mM betaine aldehyde, 50 microM 4-aminobutyraldehyde, and 50 microM 3-aminopropionaldehyde). Enzymatic activities were spectrophotometrically assayed by A340 at pH 8.0 at intervals of 0, 10, 20, 30, and 60 min after the initiation of reactions. The intact BADH2 showed high betaine aldehyde dehydrogenase activity, with a rapid increase in A340 within the first 10 min after the enzymatic reaction. In addition, intact BADH2 also showed strong 4-aminobutyraldehyde and 3-aminopropionaldehyde dehydrogenase activities.
additional information
-
Determination of aldehyde dehydrogenase activity of purified intact BADH2 and partial BADH2 using various aldehyde substrates (1 mM betaine aldehyde, 50 microM 4-aminobutyraldehyde, and 50 microM 3-aminopropionaldehyde). Enzymatic activities were spectrophotometrically assayed by A340 at pH 8.0 at intervals of 0, 10, 20, 30, and 60 min after the initiation of reactions. The intact BADH2 showed high betaine aldehyde dehydrogenase activity, with a rapid increase in A340 within the first 10 min after the enzymatic reaction. In addition, intact BADH2 also showed strong 4-aminobutyraldehyde and 3-aminopropionaldehyde dehydrogenase activities.
additional information
quantification of 2-acetyl-1-pyrroline (2AP) and other metabolites in vivo
additional information
-
quantification of 2-acetyl-1-pyrroline (2AP) and other metabolites in vivo
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
8.5 - 9
9.5
additional information
-
mutant enzyme E103Q exhibits a broader temperature optimum than the wild-type enzyme
8
activity assay
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8
-
pH 7.0: about 35% of maximal activity, pH 8.0: about 70% of maximal activity
7 - 9
-
pH 7.0: about 40% of maximal activity, pH 9.0: about 50% of maximal activity
7 - 9.5
7 - 9.5
-
pH 7.0: about 50% of maximal activity, pH 9.5: about 75% of maximal activity
7 - 9.5
-
pH 7.0: about 25% of maximal activity, pH 9.5: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
25
activity assay
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
-
20°C: about 45% of maximal activity, 40°C: about 70% of maximal activity
additional information
results indicate that the tolerance of the recombinant yeasts to high temperature stress is improved remarkably as a result of improving glycine betaine content in the yeasts expressing betaine synthesis genes from Suaeda salsa
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.4
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Bacillus halodurans, isolated from the salt pan
UniProt
brenda
Halalkalibacterium halodurans SMBPL06
Bacillus halodurans, isolated from the salt pan
UniProt
brenda
from Turpan Desert Botanical Garden of the Chinese Academy of Sciences, China
UniProt
brenda
five transgenic tomato (Lycopersicon esculentum Mill) lines T3-1, T3-3, T3-5, T3-8 and T3-9 with BADH gene from Atriplex hortensis are analysed concerning their behaviour under salt stress conditions and compared with cv. Bailichun wild type
-
-
brenda
over-producing strain carrying the structural gene for the enzyme on the plasmid pBR322
-
-
brenda
aldehyde dehydrogenase E3 isoenzyme is a betaine aldehyde dehydrogenase
-
-
brenda
susp. japonica; susp. japonica and indica; different varieties are investigated
Uniprot
brenda
several BADH gene paralogues, cv. Cadoux
UniProt
brenda
-
-
-
brenda
2 enzyme forms: BADG I and BADH II. BADH II comprises more than 60% of the total activity
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
found in all plant tissues excepting roots, expression level is highest in leaves and stems
brenda
additional information
found in all plant tissues excepting roots, expression level is highest in leaves and stems
brenda
-
higher activity in cortex than in medulla. In inner medulla, the enzyme is mainly localized in cells surrounding the tubules
brenda
found in all plant tissues excepting roots, expression level is highest in leaves and stems
brenda
the site of storage for aroma volatile 2-acetyl-1-pyrroline (2AP) are bag-like structures called epidermal papillae identified on the lower epidermis of the leaves of the species
brenda
-
leaves are used for analyzing activities of enzymes from photosystem II
brenda
found in all plant tissues excepting roots, and the transcript is detected at higher abundance in young, healthy leaves than in other tissues
brenda
find in all plant tissues excepting roots, expression level is highest in leaves and stems
brenda
found in all plant tissues excepting roots, expression level is highest in leaves and stems
brenda
additional information
primary synthesis and accumulation of glycine betaine involving the enzyme occur in young parts of plants, and it is then transported to the older regions/tissues through phloem
brenda
additional information
tissue specific enzyme expression analysis by quantitative real-time PCR
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
cytoplasmic and mitochondrial enzymes are products of the same gene
brenda
-
95% of the activity, 5% of the activity is localized in mitochondria
brenda
-
the enzyme is approximately equally distributed between the inner membrane and the intermembrane plus matrix fraction
brenda
-
matrix. Cytoplasmic and mitochondrial enzymes are products of the same gene
brenda
-
5% of the activity in mitochondrial matrix, 95% of the activity in cytosol
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
metabolism
physiological function
additional information
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. 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
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
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. 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
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
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
-
the badh2 gene alone is not sufficient enough to explain the genetic and molecular basis of fragrance in rice
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
-
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
ALDH10A8 serves as detoxification enzyme 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 enzyme plays a role in temperature stress tolerance
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 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 is a positive regulator during the response to NaCl
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
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
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
-
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
Vallaris sp.
-
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) 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
-
porcine kidney betaine aldehyde dehydrogenase (pkBADH) binds NAD+ with different affinities at each active site and the binding is K+ dependent
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
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
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
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
-
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
-
additional information
three-dimensional docking analysis of PaBADH2 with betaine aldehyde
additional information
-
three-dimensional docking analysis of PaBADH2 with betaine aldehyde
additional information
for Ile445 containing AMADHs, the existence of Asn290 rather than Thr290 leads to detectable BADH activity
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
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
-
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
Show AA Sequence and Transmembrane Helices (4464 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
117000
-
2 * 117000, betaine aldehyde dehydrogenase/choline dehydrogenase fusion protein, SDS-PAGE
230000
232000
250000
-
betaine aldehyde dehydrogenase/choline dehydrogenase fusion protein, gel filtration
54000
55000
55500
estimated by SDS-PAGE
60000
61000
63000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homotetramer
tetramer
additional information
?
-
2 * 117000, betaine aldehyde dehydrogenase/choline dehydrogenase fusion protein, SDS-PAGE
dimer
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. Key inter-subunit salt bridges contributing to dimerization are identified. E487, D491, E492, K498, and K502 form strong salt bridges with charged residues on the adjacent monomer. Specifically, the nearly permanent R430-E487 hydrogen bond (over 90%) highlights its key role in dimer association
tetramer
-
at pH 7.0 in the absence of K+ in a buffer of low ionic strength, the active tetrameric form dissociates into inactive monomers
tetramer
-
at pH 7.0 in the absence of K+ in a buffer of low ionic strength, the active tetrameric form dissociates into inactive dimers
tetramer
4 * 53940, about, sequence calculation, 4 * 54000, recombinant enzyme, SDS-PAGE
additional information
-
secondary and tertiary structure of pkBADH in presence or absence of NAD+, fluorescence quenching spectra of pkBADH titrated with variable NAD+ concentrations in presence of potassium, overview. The deconvolution data analysis shows a 13% increase in the pkBADH helical structure, a decrease of 7% in beta-sheet content and 6% in turns content during the pkBADH-NAD+ complex formation
additional information
enzyme secondary structrue analysis, pkBADH/NAD+ interaction analysis by circular dichroism (CD) and by isothermal titration calorimetry (ITC) by titrating the enzyme with NAD+, overview. pkBADH shows 17% of unordered structure, 41% of alpha-helix, and 29% of beta-sheet
additional information
-
enzyme secondary structrue analysis, pkBADH/NAD+ interaction analysis by circular dichroism (CD) and by isothermal titration calorimetry (ITC) by titrating the enzyme with NAD+, overview. pkBADH shows 17% of unordered structure, 41% of alpha-helix, and 29% of beta-sheet
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
side-chain modification Attention: controlled vocabulary for this datafield
commentary
additional information
proteolytic modification
-
transit peptide may comprise only 7 or 8 residues
proteolytic modification
-
enzyme is synthesisized as a precursor of 1200 Da higher than the mature enzyme
additional information
several truncated or recombinant transcripts of BADH1 and BADH2 emerging from an unusual post-transcriptional process have been found in barley
additional information
several truncated or recombinant transcripts of BADH1 and BADH2 emerging from an unusual post-transcriptional process have been found in rice
additional information
several truncated or recombinant transcripts of BADH1 and BADH2 emerging from an unusual post-transcriptional process have been found in rice
additional information
several truncated or recombinant transcripts of BADH1 and BADH2 emerging from an unusual post-transcriptional process have been found in wheat
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
microbatch method, in the presence of NAD+, using 0.1 M HEPES pH 7.4, 24% (w/v) PEG 4000 and 0.2 M ammonium chloride
-
BADH in the presence of 2-mercaptoethanol, glycerol, NADP+ and 150 mM K+, hanging drop vapor diffusion method, using 85 mM HEPESNaOH, pH 7.5, 8.5% (v/v) isopropanol, 17% (w/v) polyethylene glycol 4000 and 15% (v/v) glycerol, at 18°C
native and mutant enzyme C286A in complex with NADPH, hanging drop vapor diffusion method, using 85 mM HEPES/NaOH buffer, pH 7.5, 8.5% (v/v) propan-2-ol, 17% (w/v) PEG 4000, and 15% (v/v) glycerol
the three dimensional structure of betaine aldehyde dehydrogenase, in complex with glycerol, NADP+ and K+ ions, is determined at 2.1 A resolution
sitting drop vapor diffusion method, using 200 mM MgCl2,100 mM Tris pH 8.5, 20% (w/v) PEG 8000
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G1036A/Y1178F
the mutations lead to about 30% and almost complete loss of carboxylic acid reductase and aldehyde reductase activity, respectively
Y1178F
the mutation leads to a greater than 150fold loss of aldehyde reductase activity
Y811F
the mutant shows no activity with glycine betaine and wild type activity with glycine betaine aldehyde
G1036A/Y1178F
-
the mutations lead to about 30% and almost complete loss of carboxylic acid reductase and aldehyde reductase activity, respectively
-
Y1178F
-
the mutation leads to a greater than 150fold loss of aldehyde reductase activity
-
Y811F
-
the mutant shows no activity with glycine betaine and wild type activity with glycine betaine aldehyde
-
C286A
C353A
C377A
C439A
C439S
-
steady-state kinetic and structure not significantly affected, stability severely reduced
C439V
-
steady-state kinetic and structure not significantly affected, stability severely reduced
A441C
A441I
A441S
the mutant exhibits slightly reduced activity with betaine aldehyde
A441T
the mutant exhibits clearly reduced activity with betaine aldehyde
E103K
-
mutant enzyme has no activity with betaine aldehyde and 4-aminobutyraldehyde
E103Q
G234A
-
the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
G234S
G234T
-
the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
H448F
-
the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
H448F/P449M
-
the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
H448F/P449M/Y450L
-
the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
H448F/Y450L
-
the mutant demonstrates a complete loss of substrate inhibition
L161M/Q162M
-
the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
P449M/Y450L
-
the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
Q162M
-
the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
S290T
-
the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
V288D
-
the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
W456H
-
the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
Y450L
-
the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
additional information
C286A
-
cysteine 286 plays an important role in the maintenance ot the tetrameric structure
C353A
-
mutant, shows similar inactivation kinetics to the wild-type enzyme
C377A
-
mutant, shows similar inactivation kinetics to the wild-type enzyme
C439A
-
steady-state kinetic and structure not significantly affected, stability severely reduced
C439A
-
mutant, shows similar inactivation kinetics to the wild-type enzyme
A441C
-
the mutant demonstrates reduced substrate inhibition by betaine aldehyde
A441C
the mutant exhibited almost wild type activity with betaine aldehyde
A441I
-
the mutant demonstrates reduced substrate inhibition by betaine aldehyde
E103Q
-
mutant enzyme is slightly more sensitive to inhibition by NaCl but less sensitive to inhibition by (NH4)2SO4. Glycine betaine activates the wild-type enzyme but not the mutant enzyme. Mutant enzyme shows stronger inhibition by choline compared to wild-type enzyme. Wild-type enzyme shows stronger inhibition by isovaleraldehyde than the mutant enzyme.Mutant enzyme exhibits a broader temperature optimum than the wild-type enzyme. Mutant enzyme appears to be more heat labile than the wild-type enzyme. Mutant enzyme is less stable than the wild-type enzyme in the pH-range 5-11. Mutant enzyme and wild-type enzyme are protected by NAD+ against thermal inactivation in a similar manner. Neither glycine betaine nor NaCl can afford protection against thermal inactivation in the mutant enzyme whereas some protection is observed in the wild-type enzyme
G234S
the mutant shows increased activity and reduced substrate inhibition compared to the wild type enzyme
G234S
-
the mutant with reduced catalytic efficiency demonstrates reduced substrate inhibition with betaine aldehyde compared to the wild type enzyme
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
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
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
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 11
-
mutant enzyme is less stable than the wild-type enzyme in the pH-range 5-11
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
47.2 - 59.9
-
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. The first derivative analysis from the pkBADH-NAD+ complex shows a peak with a (Tm)app value of 47.2°C, the addition of 25 mM K+ increased the (Tm)app to 59.9°C, while the addition of 50 mM or 100 mM K+ provokes changes in the (Tm)app to 55.9°C or 54.9°C, respectively. Binding of NAD+ to pkBADH causes a lower thermal stability of the enzyme
50
additional information
-
mutant enzyme E103Q appears to be more heat labile than the wild-type enzyme. Mutant enzyme E103Q and wild-type enzyme are protected by NAD+ against thermal inactivation in a similar manner. Neither glycine betaine nor NaCl can afford protection against thermal inactivation in the mutant enzyme whereas some protection is observed in the wild-type enzyme
40
-
loss of activity, activity is regained, when the heated enzyme is cooled to 30°C or lower
50
-
pH 7.4, 0.01% 2-mercaptoethanol, 7 min, complete loss of activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
at the optimum pH of 8.0 the enzyme is inactivated by dilution, it is stable at pH 6.5 even at very low concentrations
-
complete loss of activity when dialyzed against 10 mM buffer, pH 8.0, addition of 20% glycerol stabilizes
-
the enzyme is stable in absence of K+ even at very low enzyme concentrations
-
total RNA of leaves subjected to RT-PCR analysis to examine the influence of environmental stress like drought, salt or heat on BADH expression. Results showed tha JcBD1 gene transcripts of those plants exposed to 30% PEG, 300 mM NaCl or 50°C heat stress were obviously higher than that of the control plants. JcBD1 mRNA levels in stress treated leaved are increased by 79% or more, as compared with the control, which strongly confirms that mRNA expression are relative to abiotic stress.
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
conformational change induced by coenzyme or the aldehyde might be important for both proper enzyme function and protection against oxidation
conformational change induced by coenzyme or the aldehyde might be important for both proper enzyme function and protection against oxidation
-
655203
conformational change induced by coenzyme or the aldehyde might be important for both proper enzyme function and protection against oxidation
-
655203
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, frozen in presence of 10 mM dithiothreitol, stable for several months without appreciable loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
For purification of the recombinant protein, cells of 500 ml culture are harvested. Pellet is suspended in lysis buffer and suspension was incubated. Following sonication, suspension is centrifuged. Clear supernatant is collected and loaded onto a Glutathione-Agarose column equilibrated with buffer (20 mM Tris-HCl (pH 8.0), 5.0 mM EDTA). The recombinant protein is eluted with elution buffer (20 mM Tris-HCl (pH 8.0), 5.0 mM EDTA, and 1.0 mM reduced glutathione). Eluted protein is collected and the purity is analyzed by 12% SDS-PAGE. To remove the GST moiety, the recombinant proteins are digested with PreScission protease.
Ni-NTA resin column chromatography, and Superdex 200 gel filtration
on GSTrap FF columns
partial
purified on Q-Sepharose fast flow and 2', 5'-ADP-Sepharose columns, 28 mg of pure protein per liter of culture are yielded
purified to homogeneity following a two-step procedure, proteins expressed in Escherichia coli
-
recombinant enzyme from Escherichia coli strain ER2566 by chitin affinity chromatography
recombinant enzyme from Escherichia coli strain M15 by anion exchange chromatography
recombinant His-tagged isozyme AMADH1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
the protein undergoes several chromatographic and dialysis steps during purification
-
using nickel-nitrilotriacetic acid agarose affinity chromatography columns after expression in E. coli
using nickel-nitrilotriacetic acid agarose affinity chromatography columns after expression in Escherichia coli
using nickel-nitrilotriacetic acid agarose after cloning and expression in Escherichia coli
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Ipomoea batatas cultivar Sushu-2 via Agrobacterium-mediated transformation
-
expressed in trifoliate orange Poncirus trifoliata by Agrobacterium-mediated transformation
-
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
-
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
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
-
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.
-
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
of genes encoding five forms of spinach enzyme: full length, mature, mutant E103Q, mutant E103K and chimera
-
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
-
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
-
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)
-
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.
-
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
-
gene BADH, Agrobacterium tumefaciens-mediated recombinant expression in Arabidopsis thaliana
-
gene BADH, Agrobacterium tumefaciens-mediated recombinant expression in Arabidopsis thaliana
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
betaine aldehyde dehydrogenase transcript levels and activity are differentially modulated by NO in light and dark growth conditions. 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. Betaine aldehyde dehydrogenase transcript levels and activity are differentially modulated by NO in light and dark growth conditions
in NaCl treated seedlings, accompanied by elevated GB accumulation, expression of LrAMADH1 is upregulated, indicating response of LrAMADH1 to salt stress in Lycium ruthenicum
mRNA expression in muscle decreases 4fold and 15fold after 7 days at low and high salinity, respectively
mRNA expression increases 2-3fold in the hepatopancreas and gills after 7 days of osmotic variation
temperature stresses induce the enzyme expression during storage with high temperature causes a significantly higher induction of enzyme expression
-
the ALDH10A8 gene is weakly induced by abscisic acid, salt, chilling (4°C), methyl viologen and dehydration
the ALDH10A9 gene is weakly induced by abscisic acid, salt, chilling (4°C), methyl viologen and dehydration
the endogenous expression of the gene is strongly induced by the treatments of high salt (250 mM NaCl), dehydration, abscisic acid (0.1 mM), heat (45°C), and cold (-4°C)
the enzyme expression is significantly induced by 200 mM NaCl and reaches the maximal level in 3 days
the expression of isozymes BADH1 and BADH2 is decreased by the submerged treatment and recovered to control (0 h) level after re-aeration
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol, Reactivation of DSF-inactivated enzyme with 10 mM 2-mercaptoethanol
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
biotechnology
energy production
the seed of the plant is the raw material for biodiesels
food industry
the BADH2 could play a role in the improvement of rice fragrance, which could lead to an enhancement in rice quality and market price
medicine
molecular biology
additional information
agriculture
-
gene expression under the control of inducible promoters is preferred in any strategy to produce transgenic plants with transgene-mediated improvements in resistance to salt.
agriculture
-
potential application, genetic engineering results in enhanced tolerance of growth of young seedlings to salt stress. Results of investigation shows that transformation with the BADH gene may benefit efforts to improve crop yields in saline, arid and semi-arid regions where plants suffer salt stress
agriculture
-
potential: the BADH gene can be cloned from Leymus chinensis under stress treatment, which indicates that its expression and regulation may play an important role in stress tolerance. Therefore, it can be transformed into other plants to obtain transgenic species with a high saline-alkali tolerance by biotechnology; as a result, it can speed up the recovering and rebuilding of saline-alkaline grassland
biotechnology
overexpression of AMADHs with high BADH activities is an important strategy to genetically engineer Solanaceae crop plants, such as tomato and tobacco, to produe glycine betaine
biotechnology
BADH overexpression in maize is beneficial for drought tolerance and the three transgenic maize lines can be used for further breeding experiments. The agronomic traits of transgenic maize are not affected by the overexpression of BADH
medicine
Pseudomonas aeruginosa is an important pathogen, glycine betaine could play an important physiological role under the conditions present in the infection sites
medicine
-
betaine aldehyde dehydrogenase is a potential target for antimicrobial agents against Pseudomonas aeruginosa
molecular biology
BADH application as a marker for chloroplast engineering without using antibiotic can avoid transferring antibiotic genes from the plant and thus assists to allay public concern regarding genetic modifications
molecular biology
BADH application as a marker for chloroplast engineering without using antibiotic can avoid transferring antibiotic genes from the plant and thus assists to allay public concern regarding genetic modifications
molecular biology
BADH application as a marker for chloroplast engineering without using antibiotic can avoid transferring antibiotic genes from the plant and thus assists to allay public concern regarding genetic modifications
molecular biology
BADH application as a marker for chloroplast engineering without using antibiotic can avoid transferring antibiotic genes from the plant and thus assists to allay public concern regarding genetic modifications
molecular biology
-
BADH application as a marker for chloroplast engineering without using antibiotic can avoid transferring antibiotic genes from the plant and thus assists to allay public concern regarding genetic modifications
molecular biology
BADH application as a marker for chloroplast engineering without using antibiotic can avoid transferring antibiotic genes from the plant and thus assists to allay public concern regarding genetic modifications
molecular biology
Q53CF4
BADH application as a marker for chloroplast engineering without using antibiotic can avoid transferring antibiotic genes from the plant and thus assists to allay public concern regarding genetic modifications
molecular biology
-
BADH application as a marker for chloroplast engineering without using antibiotic can avoid transferring antibiotic genes from the plant and thus assists to allay public concern regarding genetic modifications
molecular biology
BADH application as a marker for chloroplast engineering without using antibiotic can avoid transferring antibiotic genes from the plant and thus assists to allay public concern regarding genetic modifications
molecular biology
Vallaris sp.
-
BADH application as a marker for chloroplast engineering without using antibiotic can avoid transferring antibiotic genes from the plant and thus assists to allay public concern regarding genetic modifications
molecular biology
BADH application as a marker for chloroplast engineering without using antibiotic can avoid transferring antibiotic genes from the plant and thus assists to allay public concern regarding genetic modifications
molecular biology
-
BADH application as a marker for chloroplast engineering without using antibiotic can avoid transferring antibiotic genes from the plant and thus assists to allay public concern regarding genetic modifications
additional information
BADH isolated from spinach is successfully utilised for selection of chloroplast transformation of tobacco in order to prevent the risk of transferring antibiotic resistance genes to gut microbes or the environment
additional information
nitric oxide and light co-regulate glycine betaine homeostasis in sunflower seedling cotyledons by modulating betaine aldehyde dehydrogenase transcript levels and activity
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Release 2026.1 (March 2026)
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