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Information on EC 1.2.1.8 - betaine-aldehyde dehydrogenase
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1.2.1.8 betaine-aldehyde dehydrogenaseIUBMB 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).
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Word Map
- 1.2.1.8
-
badhs
- choline
-
osmoprotectant
-
fragrant
- aroma
-
2-acetyl-1-pyrroline
-
basmati
-
spinacia
- glycinebetaine
-
halophyte
- suaeda
- aminoaldehyde
- amaranthus
- 3-aminopropionaldehyde
- 4-aminobutyraldehyde
-
jasmine
- medicine
- liaotungensis
- hypochondriacus
- agriculture
- energy production
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
ALD10, aldehyde dehydrogenase, ALDH10, ALDH10A8, ALDH10A9, BADH, BADH1, BADH2, badh2-E2, badh2-E7, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
-
-
-
-
PaBADH
ZBD1
-
Zoysia betaine aldehyde dehydrogenase 1
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BADH
-
-
-
-
BADH
-
betaine aldehyde dehydrogenase
-
-
-
-
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+
ping-pong mechanism
-
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
iso-ordered bi-bi steady state mechanism
-
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
iso-ordered bi-bi steady state mechanism; NAD+ is the first substrate to bind to the enzyme and NADH is the last product to dissociate from it
-
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+
steady-state ordered bi bi or rapid equilibrium mechanism
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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
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betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
catalyzes the last irreversible step in the synthesis of the osmoprotector glycine betaine
-
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
catalyzes the last step of the two-step oxidation
-
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+
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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-
-
-
redox reaction
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-
-
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reduction
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-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-dimethylsulfoniopropionaldehyde + NAD+ + O2
3-dimethylsulfoniopropionate + NADH
-
steady state bi bi mechanism with ordered addition of substrates and random release of products
-
-
ir
3-N-trimethylaminopropionaldehyde + NAD+ + H2O
3-N-trimethylaminopropanoate + NADH + H+
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-
-
-
?
3-N-trimethylaminopropionaldehyde + NAD+ + H2O
3-N-trimethylaminopropionate + NADH + H+
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH + H+
-
-
-
?
4-N-trimethylaminobutyraldehyde + NAD+ + H2O
4-N-trimethylaminobutyrate + NADH + H+
-
-
-
-
?
4-N-trimethylaminobutyraldehyde + NAD+ + H2O
4-N-trmethylaminobutanoate + NADH + H+
-
-
-
-
?
4-trimethylaminobutyraldehyde + NAD+ + H2O
3-trimethylaminobutyrate + NADH
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-
-
-
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + 2 H+
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-
-
-
ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + 2 H+
-
-
-
r
betaine aldehyde + NADP+ + H2O
glycine betaine + NADPH + H+
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-
-
-
ir
butyraldehyde + NAD+ + H2O
butyrate + NADH
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at 40% of the activity with betaine aldehyde
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-
?
glyceraldehyde + NAD+ + H2O
glycerate + NADH
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at 30% of the activity with betaine aldehyde
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
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-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionic acid + NADH + H+
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-
-
-
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
-
no activity
-
-
-
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
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-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
-
-
-
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acetaldehyde + NAD+ + H2O
acetate + NADH + H+
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at 20% of the activity with betaine aldehyde
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-
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
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-
-
-
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
-
-
-
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ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
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enzyme catalyzes the final irreversible step in the synthesis of glycine betaine
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-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
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the enzyme is involved in the metabolism of choline, induced during growth on choline
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-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
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the enzyme is involved in the metabolism of choline, induced during growth on choline
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-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
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-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
highly specific for betaine aldehyde
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-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
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enzyme of the osmoregulatory choline-glycine betaine pathway
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-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
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the salt tolerance is an essential property for the enzyme participating in the cellular synthesis of an osmoprotectant
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ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
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synthesis of betaine
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-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
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reverse reaction not detected
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ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
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preferentially uses NADP+ over NAD+
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-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
enzyme catalyzes the last, irreversible step in the synthesis of the osmoprotectant glycine betaine from choline, also obligatory step in the assimilation of carbon and nitrogen when bacteria are growing in choline or choline precursors
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ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
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inducible enzyme accumulates in the presence of choline, acetylcholine or betaine in the medium
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-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
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reverse reaction not detected
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-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
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inducible enzyme accumulates in the presence of choline, acetylcholine or betaine in the medium
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-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
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-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
the enzyme has an important function in the metabolism of choline to betaine, a major osmolyte. Betaine is also important in mammalian organisms as a major methyl group donor and nitrogen source
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-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
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the age-related acceleration in conversion of choline into betaine probably tends to diminish unesterified choline concentrations
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
enzyme is induced several-fold by salinization
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-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
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-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
equilibrium of the reaction strongly favours betaine formation
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-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
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enzyme is induced several-fold by salinization
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-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
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-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
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+
-
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accumulation of betaine is a strategy of plants to survive drought, salinity, and extreme temperatures
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
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+
-
the enzyme catalyzes the second step in the synthesis of the osmoprotectant glycine betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
the osmoprotective compound glycine betaine is produced from choline by two enzymes. Choline dehydrogenase oxidizes choline to betaine aldehyde and then further to glycine betaine, while betaine aldehyde dehydrogenase facilitates the conversion of betaine aldehyde to glycine betaine
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-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
more active on medium-chain aldehydes than on betaine aldehyde
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-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
belongs to the NAD-dependent dehydrogenase family, characterized by the typical aldehyde substrate binding domain
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
barley plants synthesize GB through catalytic reaction of the functional BADH protein, even though a large number of incorrectly processed BADH transcripts observed may considerably reduce the precise gene.
-
ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
barley plants synthesize glycine betaine through catalytic reaction of the functional BADH protein, even though a large number of incorrectly processed BADH transcripts observe in this study may considerably reduce the precise gene
-
ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
B2BBY6
-
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+
Q153G6
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
the appropriate level of glycine betaine may be regulated at both the transcriptional and posttranscriptional levels. Namely, the transcription is induced abundantly in response to the osmotic stresses, while the proper amount of precise gene products is balanced by posttranscriptional processing
-
ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
the appropriate level of glycine may be regulated at both the transcriptional and posttranscriptional levels; namely, the transcription is induced abundantly in response to the osmotic stresses, while the proper amount of precise gene products is balanced by posttranscriptional processing
-
ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
Results demonstrate that accumulation of glycine betaine in vivo in the chloroplast in tobacco plants by introducing the BADH gene for betaine aldehyde dehydrogenase from spinach resulted in increased tolerance of growth of young seedlings to salt stress. Furthermore results demonstrate that accumulation of glycine betaine in vivo leads to increased tolerance of CO2 assimilation to salt stress.
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
accumulated in many species in response to salt stress. It protects the cell by maintaining an osmotic balance with the environment and by stabilizing quaternary structure of complex proteins
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
glycine betaine synthesis; two-step oxidation involving choline monooxygenase and BADH
recombinant yeasts transformed with the two genes CMO and BADH exhibited higher tolerance to salt, methanol and high temperature stress.
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
NAD+ is preferred over NADP+
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
preferentially uses NADP+ over NAD+
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
no activity with NAD+
-
-
-
betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
no activity with NAD+
-
-
-
betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
75% of the activity with NAD+
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
25% of the maximal activity with NAD+
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
-
more active on medium-chain aldehydes than on betaine aldehyde
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
-
low activity with NADP+
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
-
the enzyme has evolved a complex mechanism, involving several conformational rearrangements of the active site, to suit the reactivity of the essential thiol to the availability of dinucleotide and sunstrate
-
-
ir
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
the enzyme is also active with NADP+, but the NAD-supported activity is at least 10times higher
-
-
?
additional information
?
-
2-acetyl-1-pyrroline, the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele badh2-E7, induces 2-acetyl-1-pyrroline formation
-
-
-
additional information
?
-
2-acetyl-1-pyrroline, the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele badh2-E7, induces 2-acetyl-1-pyrroline formation
-
-
-
additional information
?
-
2-acetyl-1-pyrroline, the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele badh2-E7, induces 2-acetyl-1-pyrroline formation
-
-
-
additional information
?
-
2-acetyl-1-pyrroline; the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele, badh2-E2, induces 2-acetyl-1-pyrroline formation
-
-
-
additional information
?
-
2-acetyl-1-pyrroline; the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele, badh2-E2, induces 2-acetyl-1-pyrroline formation
-
-
-
additional information
?
-
2-acetyl-1-pyrroline; the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele, badh2-E2, induces 2-acetyl-1-pyrroline formation
-
-
-
additional information
?
-
dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. Because the absence of BADH2 protein results in fragrance, this suggests that Badh2 is not directly involved in biosynthesis. Alternative possibilities to explain the effect of BADH2 are that the BADH2 enzyme is involved in a competing pathway in which one of the 2-acetyl-1-pyrroline precursors serves as a BADH2 substrate or that BADH2 participates in 2-acetyl-1-pyrroline catabolism. The intact 503 amino acid BADH2 encoded by the complete Badh2 gene inhibits 2-acetyl-1-pyrroline biosynthesis by converting 4-aminobutyraldehyde to gamma-aminobutyric acid, whereas the absence of BADH2 due to nonfunctional badh2 alleles results in AB-ald accumulation and thus turns on the pathway toward 2-acetyl-1-pyrroline biosynthesis.
-
-
-
additional information
?
-
dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. Because the absence of BADH2 protein results in fragrance, this suggests that Badh2 is not directly involved in biosynthesis. Alternative possibilities to explain the effect of BADH2 are that the BADH2 enzyme is involved in a competing pathway in which one of the 2-acetyl-1-pyrroline precursors serves as a BADH2 substrate or that BADH2 participates in 2-acetyl-1-pyrroline catabolism. The intact 503 amino acid BADH2 encoded by the complete Badh2 gene inhibits 2-acetyl-1-pyrroline biosynthesis by converting 4-aminobutyraldehyde to gamma-aminobutyric acid, whereas the absence of BADH2 due to nonfunctional badh2 alleles results in AB-ald accumulation and thus turns on the pathway toward 2-acetyl-1-pyrroline biosynthesis.
-
-
-
additional information
?
-
dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. Because the absence of BADH2 protein results in fragrance, this suggests that Badh2 is not directly involved in biosynthesis. Alternative possibilities to explain the effect of BADH2 are that the BADH2 enzyme is involved in a competing pathway in which one of the 2-acetyl-1-pyrroline precursors serves as a BADH2 substrate or that BADH2 participates in 2-acetyl-1-pyrroline catabolism. The intact 503 amino acid BADH2 encoded by the complete Badh2 gene inhibits 2-acetyl-1-pyrroline biosynthesis by converting 4-aminobutyraldehyde to gamma-aminobutyric acid, whereas the absence of BADH2 due to nonfunctional badh2 alleles results in AB-ald accumulation and thus turns on the pathway toward 2-acetyl-1-pyrroline biosynthesis.
-
-
-
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
additional information
?
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ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
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-
-
additional information
?
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-
isozyme BADH1 catalyzes the oxidation of acetaldehyde efficiently, while the activity of isozyme BADH2 is extremely low
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-
-
additional information
?
-
-
no activity with 3-dimethylsulfoniopropionaldehyde
-
-
-
additional information
?
-
-
BADH can also use as substrates aminoaldehydes and other quaternary ammonium and tertiary sulfonium compounds, thereby participating in polyamine catabolism and in the synthesis of gamma-aminobutyrate, carnitine, and 3-dimethylsulfoniopropionate
-
-
-
additional information
?
-
-
betaine aldehyde dehydrogenase gene expression in leaves increases with salt stress
-
-
-
additional information
?
-
-
betaine aldehyde dehydrogenase gene expression in leaves increases with salt stress
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH + H+
B3VMC0, B3VMC1, B3VMC2
-
-
-
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + 2 H+
-
-
-
-
ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + 2 H+
Q9HTJ1
-
-
-
r
betaine aldehyde + NADP+ + H2O
glycine betaine + NADPH + H+
-
-
-
-
ir
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
Q9S795, Q9STS1
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
B3VMC0, B3VMC1, B3VMC2
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
Q9S795, Q9STS1
-
-
-
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
-
-
-
-
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
-
-
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
enzyme catalyzes the final irreversible step in the synthesis of glycine betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
the enzyme is involved in the metabolism of choline, induced during growth on choline
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
the enzyme is involved in the metabolism of choline, induced during growth on choline
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
enzyme of the osmoregulatory choline-glycine betaine pathway
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
the salt tolerance is an essential property for the enzyme participating in the cellular synthesis of an osmoprotectant
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
enzyme catalyzes the last, irreversible step in the synthesis of the osmoprotectant glycine betaine from choline, also obligatory step in the assimilation of carbon and nitrogen when bacteria are growing in choline or choline precursors
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
inducible enzyme accumulates in the presence of choline, acetylcholine or betaine in the medium
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
inducible enzyme accumulates in the presence of choline, acetylcholine or betaine in the medium
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
the enzyme has an important function in the metabolism of choline to betaine, a major osmolyte. Betaine is also important in mammalian organisms as a major methyl group donor and nitrogen source
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
the age-related acceleration in conversion of choline into betaine probably tends to diminish unesterified choline concentrations
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
enzyme is induced several-fold by salinization
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
enzyme is induced several-fold by salinization
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
last step in betaine synthesis, a nontoxic or protective osmolyte under saline or dry conditions
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
-
-
accumulation of betaine is a strategy of plants to survive drought, salinity, and extreme temperatures
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
regulates osmotic pressure and protects enzyme activities; the transgenic plants have a higher accumulation of betaine
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
the enzyme catalyzes the second step in the synthesis of the osmoprotectant glycine betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
the osmoprotective compound glycine betaine is produced from choline by two enzymes. Choline dehydrogenase oxidizes choline to betaine aldehyde and then further to glycine betaine, while betaine aldehyde dehydrogenase facilitates the conversion of betaine aldehyde to glycine betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
B3VMC0, B3VMC1, B3VMC2
belongs to the NAD-dependent dehydrogenase family, characterized by the typical aldehyde substrate binding domain
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
Q9S795, Q9STS1
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
Q94IC0, Q94IC1
-
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+
Q94IC0, Q94IC1
-
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+
B2BBY6
-
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+
Q153G6
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
O24174, Q84LK3
-
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+
O24174, Q84LK3
-
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+
-
-
Results demonstrate that accumulation of glycine betaine in vivo in the chloroplast in tobacco plants by introducing the BADH gene for betaine aldehyde dehydrogenase from spinach resulted in increased tolerance of growth of young seedlings to salt stress. Furthermore results demonstrate that accumulation of glycine betaine in vivo leads to increased tolerance of CO2 assimilation to salt stress.
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
accumulated in many species in response to salt stress. It protects the cell by maintaining an osmotic balance with the environment and by stabilizing quaternary structure of complex proteins
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
Q155V4
glycine betaine synthesis; two-step oxidation involving choline monooxygenase and BADH
recombinant yeasts transformed with the two genes CMO and BADH exhibited higher tolerance to salt, methanol and high temperature stress.
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
Q6BD86, Q6BD88, Q6BD90, Q6BD91, Q6BD93, Q6BD95, Q6BD99, Q6BDA3, Q6BDA4
-
-
-
?
additional information
?
-
B3VMC0
2-acetyl-1-pyrroline, the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele badh2-E7, induces 2-acetyl-1-pyrroline formation
-
-
-
additional information
?
-
B3VMC1
2-acetyl-1-pyrroline, the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele badh2-E7, induces 2-acetyl-1-pyrroline formation
-
-
-
additional information
?
-
B3VMC2
2-acetyl-1-pyrroline, the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele badh2-E7, induces 2-acetyl-1-pyrroline formation
-
-
-
additional information
?
-
B3VMC0
2-acetyl-1-pyrroline; the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele, badh2-E2, induces 2-acetyl-1-pyrroline formation
-
-
-
additional information
?
-
B3VMC1
2-acetyl-1-pyrroline; the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele, badh2-E2, induces 2-acetyl-1-pyrroline formation
-
-
-
additional information
?
-
B3VMC2
2-acetyl-1-pyrroline; the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele, badh2-E2, induces 2-acetyl-1-pyrroline formation
-
-
-
additional information
?
-
B3VMC0
dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. Because the absence of BADH2 protein results in fragrance, this suggests that Badh2 is not directly involved in biosynthesis. Alternative possibilities to explain the effect of BADH2 are that the BADH2 enzyme is involved in a competing pathway in which one of the 2-acetyl-1-pyrroline precursors serves as a BADH2 substrate or that BADH2 participates in 2-acetyl-1-pyrroline catabolism. The intact 503 amino acid BADH2 encoded by the complete Badh2 gene inhibits 2-acetyl-1-pyrroline biosynthesis by converting 4-aminobutyraldehyde to gamma-aminobutyric acid, whereas the absence of BADH2 due to nonfunctional badh2 alleles results in AB-ald accumulation and thus turns on the pathway toward 2-acetyl-1-pyrroline biosynthesis.
-
-
-
additional information
?
-
B3VMC1
dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. Because the absence of BADH2 protein results in fragrance, this suggests that Badh2 is not directly involved in biosynthesis. Alternative possibilities to explain the effect of BADH2 are that the BADH2 enzyme is involved in a competing pathway in which one of the 2-acetyl-1-pyrroline precursors serves as a BADH2 substrate or that BADH2 participates in 2-acetyl-1-pyrroline catabolism. The intact 503 amino acid BADH2 encoded by the complete Badh2 gene inhibits 2-acetyl-1-pyrroline biosynthesis by converting 4-aminobutyraldehyde to gamma-aminobutyric acid, whereas the absence of BADH2 due to nonfunctional badh2 alleles results in AB-ald accumulation and thus turns on the pathway toward 2-acetyl-1-pyrroline biosynthesis.
-
-
-
additional information
?
-
B3VMC2
dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. Because the absence of BADH2 protein results in fragrance, this suggests that Badh2 is not directly involved in biosynthesis. Alternative possibilities to explain the effect of BADH2 are that the BADH2 enzyme is involved in a competing pathway in which one of the 2-acetyl-1-pyrroline precursors serves as a BADH2 substrate or that BADH2 participates in 2-acetyl-1-pyrroline catabolism. The intact 503 amino acid BADH2 encoded by the complete Badh2 gene inhibits 2-acetyl-1-pyrroline biosynthesis by converting 4-aminobutyraldehyde to gamma-aminobutyric acid, whereas the absence of BADH2 due to nonfunctional badh2 alleles results in AB-ald accumulation and thus turns on the pathway toward 2-acetyl-1-pyrroline biosynthesis.
-
-
-
additional information
?
-
O24174
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
additional information
?
-
Q84LK3
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
additional information
?
-
-
betaine aldehyde dehydrogenase gene expression in leaves increases with salt stress
-
-
-
additional information
?
-
-
betaine aldehyde dehydrogenase gene expression in leaves increases with salt stress
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
; The BADH2 enzyme is predicted to contain three domains: NAD binding, substrate binding, and oligomerization domain; The BADH2 enzyme is predicted to contain three domains: NAD binding, substrate binding, and oligomerization domain
NAD+
-
BADH uses NAD+ with the same efficiency as NADP+; PaBADH uses NADP+ with the same efficiency as NAD+
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+
-
-
NADP+
-
BADH uses NADP+ with the same efficiency as NAD+; PaBADH uses NADP+ with the same efficiency as 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+
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-
B2BBY6
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
Na+
-
results indicate that transgenic plants have a lower Na+ accumulation than the wild type under saline conditions
Na+
B2BBY6
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
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-methylmethanesulfonate
-
the effect of the thiol reagent MMTS on the native enzyme structure of the wild type enzyme and the mutants is examined
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
-
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.
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
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
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
B2BBY6
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; 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
NaCl
at a concentration of 0.1 M, expression of BADH1 is increased; at a concentration of 0.1 M, expression of BADH2 is increased
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Cardiomegaly
Betaine Aldehyde Dehydrogenase expression during physiological cardiac hypertrophy induced by pregnancy.
Diabetes Complications
Methylglyoxal metabolism and diabetic complications: roles of aldose reductase, glyoxalase-I, betaine aldehyde dehydrogenase and 2-oxoaldehyde dehydrogenase.
Foot-and-Mouth Disease
Co-ordinate expression of glycine betaine synthesis genes linked by the FMDV 2A region in a single open reading frame in Pichia pastoris.
Infections
Betaine aldehyde dehydrogenase from Pseudomonas aeruginosa: cloning, over-expression in Escherichia coli, and regulation by choline and salt.
Infections
Disulfiram irreversibly aggregates betaine aldehyde dehydrogenase--a potential target for antimicrobial agents against Pseudomonas aeruginosa.
Infections
Inactivation of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa and Amaranthus hypochondriacus L. leaves by disulfiram.
Infections
The crystal structure of a ternary complex of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa Provides new insight into the reaction mechanism and shows a novel binding mode of the 2'-phosphate of NADP+ and a novel cation binding site.
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
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
-
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
0.17
Betaine aldehyde
-
mutant enzyme G234S, at pH 8.0 and 30°C; wild type enzyme, at pH 8.0 and 30°C
0.23
Betaine aldehyde
-
isozyme BADH2, pH and temperature not specified in the publication
0.291
Betaine aldehyde
-
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
1.12
NAD+
-
mutant enzyme G234A, at pH 8.0 and 30°C; mutant enzyme H448F/P449M, at pH 8.0 and 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.8
Betaine aldehyde
-
mutant enzyme H448F/P449M/Y450L, at pH 8.0 and 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.39
Betaine aldehyde
-
mutant enzyme H448F/P449M/Y450L, at pH 8.0 and 30°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.34
Betaine aldehyde
-
pH and temperature not specified in the publication
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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
B2BBY6
activities assayed in 400 ml of reaction mixture consisting of 20 mM Tris–HCl 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.
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE