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Information on EC 1.2.1.8 - betaine-aldehyde dehydrogenase and Organism(s) Oryza sativa and UniProt Accession O24174
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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
- 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
The taxonomic range for the selected organisms is: Oryza sativa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
badh2, badh1, pabadh, osbadh2, betaine-aldehyde dehydrogenase, betaine aldehyde dehydrogenase 2, osbadh1, pkbadh, badh2-e7, badh2-e2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BADH
BADH
BADH1
BADH2
badh2-E2
recessive allele, truncated form, with a 7-bp deletion in exon 2 (82 residues)
betaine aldehyde dehydrogenase
betaine aldehyde oxidase
-
-
-
-
dehydrogenase, betaine aldehyde
-
-
-
-
BADH
-
-
-
-
betaine aldehyde dehydrogenase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
the enzyme catalyzes the second step of the two-step conversion of choline into glycine betaine
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
oxidation
reduction
-
-
-
-
oxidation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -, -, -
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).
CAS REGISTRY NUMBER
COMMENTARY
9028-90-4
-
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
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
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
-
-
-
?
3-N-trimethylaminopropionaldehyde + NAD+ + H2O
3-N-trimethylaminopropionate + NADH + H+
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH + H+
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
-
-
-
-
?
4-N-trimethylaminobutyraldehyde + NAD+ + H2O
4-N-trimethylaminobutyrate + NADH + H+
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
belongs to the NAD-dependent dehydrogenase family, characterized by the typical aldehyde substrate binding domain
-
-
?
betaine aldehyde + NAD+ + H2O
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
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
2-acetyl-1-pyrroline, the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele badh2-E7, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
2-acetyl-1-pyrroline, the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele badh2-E7, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
2-acetyl-1-pyrroline, the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele badh2-E7, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
-
2-acetyl-1-pyrroline, the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele badh2-E7, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
2-acetyl-1-pyrroline; the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele, badh2-E2, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
2-acetyl-1-pyrroline; the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele, badh2-E2, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
2-acetyl-1-pyrroline; the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele, badh2-E2, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
-
2-acetyl-1-pyrroline; the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele, badh2-E2, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. Because the absence of BADH2 protein results in fragrance, this suggests that Badh2 is not directly involved in biosynthesis. Alternative possibilities to explain the effect of BADH2 are that the BADH2 enzyme is involved in a competing pathway in which one of the 2-acetyl-1-pyrroline precursors serves as a BADH2 substrate or that BADH2 participates in 2-acetyl-1-pyrroline catabolism. The intact 503 amino acid BADH2 encoded by the complete Badh2 gene inhibits 2-acetyl-1-pyrroline biosynthesis by converting 4-aminobutyraldehyde to gamma-aminobutyric acid, whereas the absence of BADH2 due to nonfunctional badh2 alleles results in AB-ald accumulation and thus turns on the pathway toward 2-acetyl-1-pyrroline biosynthesis.
-
-
?
additional information
?
-
dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. Because the absence of BADH2 protein results in fragrance, this suggests that Badh2 is not directly involved in biosynthesis. Alternative possibilities to explain the effect of BADH2 are that the BADH2 enzyme is involved in a competing pathway in which one of the 2-acetyl-1-pyrroline precursors serves as a BADH2 substrate or that BADH2 participates in 2-acetyl-1-pyrroline catabolism. The intact 503 amino acid BADH2 encoded by the complete Badh2 gene inhibits 2-acetyl-1-pyrroline biosynthesis by converting 4-aminobutyraldehyde to gamma-aminobutyric acid, whereas the absence of BADH2 due to nonfunctional badh2 alleles results in AB-ald accumulation and thus turns on the pathway toward 2-acetyl-1-pyrroline biosynthesis.
-
-
?
additional information
?
-
dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. Because the absence of BADH2 protein results in fragrance, this suggests that Badh2 is not directly involved in biosynthesis. Alternative possibilities to explain the effect of BADH2 are that the BADH2 enzyme is involved in a competing pathway in which one of the 2-acetyl-1-pyrroline precursors serves as a BADH2 substrate or that BADH2 participates in 2-acetyl-1-pyrroline catabolism. The intact 503 amino acid BADH2 encoded by the complete Badh2 gene inhibits 2-acetyl-1-pyrroline biosynthesis by converting 4-aminobutyraldehyde to gamma-aminobutyric acid, whereas the absence of BADH2 due to nonfunctional badh2 alleles results in AB-ald accumulation and thus turns on the pathway toward 2-acetyl-1-pyrroline biosynthesis.
-
-
?
additional information
?
-
-
dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. Because the absence of BADH2 protein results in fragrance, this suggests that Badh2 is not directly involved in biosynthesis. Alternative possibilities to explain the effect of BADH2 are that the BADH2 enzyme is involved in a competing pathway in which one of the 2-acetyl-1-pyrroline precursors serves as a BADH2 substrate or that BADH2 participates in 2-acetyl-1-pyrroline catabolism. The intact 503 amino acid BADH2 encoded by the complete Badh2 gene inhibits 2-acetyl-1-pyrroline biosynthesis by converting 4-aminobutyraldehyde to gamma-aminobutyric acid, whereas the absence of BADH2 due to nonfunctional badh2 alleles results in AB-ald accumulation and thus turns on the pathway toward 2-acetyl-1-pyrroline biosynthesis.
-
-
?
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
-
isozyme BADH1 catalyzes the oxidation of acetaldehyde efficiently, while the activity of isozyme BADH2 is extremely low
-
-
?
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
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
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH + H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
belongs to the NAD-dependent dehydrogenase family, characterized by the typical aldehyde substrate binding domain
-
-
?
betaine aldehyde + NAD+ + H2O
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
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
2-acetyl-1-pyrroline, the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele badh2-E7, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
2-acetyl-1-pyrroline, the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele badh2-E7, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
2-acetyl-1-pyrroline, the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele badh2-E7, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
-
2-acetyl-1-pyrroline, the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele badh2-E7, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
2-acetyl-1-pyrroline; the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele, badh2-E2, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
2-acetyl-1-pyrroline; the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele, badh2-E2, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
2-acetyl-1-pyrroline; the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele, badh2-E2, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
-
2-acetyl-1-pyrroline; the presence of a dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. By contrast, the recessive allele, badh2-E2, induces 2-acetyl-1-pyrroline formation
-
-
?
additional information
?
-
dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. Because the absence of BADH2 protein results in fragrance, this suggests that Badh2 is not directly involved in biosynthesis. Alternative possibilities to explain the effect of BADH2 are that the BADH2 enzyme is involved in a competing pathway in which one of the 2-acetyl-1-pyrroline precursors serves as a BADH2 substrate or that BADH2 participates in 2-acetyl-1-pyrroline catabolism. The intact 503 amino acid BADH2 encoded by the complete Badh2 gene inhibits 2-acetyl-1-pyrroline biosynthesis by converting 4-aminobutyraldehyde to gamma-aminobutyric acid, whereas the absence of BADH2 due to nonfunctional badh2 alleles results in AB-ald accumulation and thus turns on the pathway toward 2-acetyl-1-pyrroline biosynthesis.
-
-
?
additional information
?
-
dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. Because the absence of BADH2 protein results in fragrance, this suggests that Badh2 is not directly involved in biosynthesis. Alternative possibilities to explain the effect of BADH2 are that the BADH2 enzyme is involved in a competing pathway in which one of the 2-acetyl-1-pyrroline precursors serves as a BADH2 substrate or that BADH2 participates in 2-acetyl-1-pyrroline catabolism. The intact 503 amino acid BADH2 encoded by the complete Badh2 gene inhibits 2-acetyl-1-pyrroline biosynthesis by converting 4-aminobutyraldehyde to gamma-aminobutyric acid, whereas the absence of BADH2 due to nonfunctional badh2 alleles results in AB-ald accumulation and thus turns on the pathway toward 2-acetyl-1-pyrroline biosynthesis.
-
-
?
additional information
?
-
dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. Because the absence of BADH2 protein results in fragrance, this suggests that Badh2 is not directly involved in biosynthesis. Alternative possibilities to explain the effect of BADH2 are that the BADH2 enzyme is involved in a competing pathway in which one of the 2-acetyl-1-pyrroline precursors serves as a BADH2 substrate or that BADH2 participates in 2-acetyl-1-pyrroline catabolism. The intact 503 amino acid BADH2 encoded by the complete Badh2 gene inhibits 2-acetyl-1-pyrroline biosynthesis by converting 4-aminobutyraldehyde to gamma-aminobutyric acid, whereas the absence of BADH2 due to nonfunctional badh2 alleles results in AB-ald accumulation and thus turns on the pathway toward 2-acetyl-1-pyrroline biosynthesis.
-
-
?
additional information
?
-
-
dominant Badh2 allele encoding betaine aldehyde dehydrogenase inhibits the synthesis of 2-acetyl-1-pyrroline, a potent flavor component in rice fragrance. Because the absence of BADH2 protein results in fragrance, this suggests that Badh2 is not directly involved in biosynthesis. Alternative possibilities to explain the effect of BADH2 are that the BADH2 enzyme is involved in a competing pathway in which one of the 2-acetyl-1-pyrroline precursors serves as a BADH2 substrate or that BADH2 participates in 2-acetyl-1-pyrroline catabolism. The intact 503 amino acid BADH2 encoded by the complete Badh2 gene inhibits 2-acetyl-1-pyrroline biosynthesis by converting 4-aminobutyraldehyde to gamma-aminobutyric acid, whereas the absence of BADH2 due to nonfunctional badh2 alleles results in AB-ald accumulation and thus turns on the pathway toward 2-acetyl-1-pyrroline biosynthesis.
-
-
?
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
The BADH2 enzyme is predicted to contain three domains: NAD binding, substrate binding, and oligomerization domain
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaCl
0.5 M, firstly, expression of OsBADH1 is increased under salt stress conditions, but at high concentrations, expression has been inhibited.
NaCl
0.5 M, expression of OsBADH2 is increased under salt stress conditions, but at high concentrations, expression is inhibited.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0012
3-aminopropionaldehyde
-
isozyme BADH2, pH and temperature not specified in the publication
0.017
3-aminopropionaldehyde
-
isozyme BADH1, pH and temperature not specified in the publication
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
0.0078
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
0.23
Betaine aldehyde
-
isozyme BADH2, pH and temperature not specified in the publication
2.6
Betaine aldehyde
-
isozyme BADH1, pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
susp. japonica; susp. japonica and indica; different varieties are investigated
Uniprot
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
physiological function
-
BADH1 is possibly involved in acetaldehyde oxidation in rice plant peroxisomes
physiological function
-
betaine aldehyde dehydrogenase gene BADH2 is associated with the fragrant phenotype in rice
physiological function
-
the badh2 gene alone is not sufficient enough to explain the genetic and molecular basis of fragrance in rice
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification Attention: controlled vocabulary for this datafield
commentary
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
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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.
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.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chen, S.; Yang, Y.; Shi, W.; Ji, Q.; He, F.; Zhang, Z.; Cheng, Z.; Liu, X.; Xu, M.
Badh2, encoding betaine aldehyde dehydrogenase, inhibits the biosynthesis of 2-scetyl-1-pyrroline, a major component in rice fragrance
Plant Cell
20
1850-1861
2008
Oryza sativa (B3VMC0), Oryza sativa (B3VMC1), Oryza sativa (B3VMC2), Oryza sativa
Niu, X.; Zheng, W.; Lu, B.R.; Ren, G.; Huang, W.; Wang, S.; Liu, J.; Tang, Z.; Luo, D.; Wang, Y.; Liu, Y.
An unusual posttranscriptional processing in two betaine aldehyde dehydrogenase loci of cereal crops directed by short, direct repeats in response to stress conditions
Plant Physiol.
143
1929-1942
2007
Arabidopsis thaliana (Q9S795), Arabidopsis thaliana (Q9STS1), Hordeum vulgare (Q94IC0), Hordeum vulgare (Q94IC1), Oryza sativa (O24174), Oryza sativa (Q84LK3), Solanum lycopersicum, Spinacia oleracea (P17202), Triticum aestivum, Triticum aestivum (Q8LGQ9), Zea mays (Q53CF4)
Gao, C.; Han, B.
Evolutionary and expression study of the aldehyde dehydrogenase (ALDH) gene superfamily in rice (Oryza sativa)
Gene
431
86-94
2009
Oryza sativa (O24174), Oryza sativa (Q84LK3)
Fitzgerald, T.L.; Waters, D.L.; Henry, R.J.
Betaine aldehyde dehydrogenase in plants
Plant Biol.
11
119-130
2009
Avena sativa, Beta vulgaris, Embryophyta, Hordeum vulgare, Oryza sativa, Pisum sativum, Zoysia tenuifolia
Sakthivel, K.; Sundaram, R.M.; Shobha Rani, N.; Balachandran, S.M.; Neeraja, C.N.
Genetic and molecular basis of fragrance in rice
Biotechnol. Adv.
27
468-473
2009
Oryza sativa
Mitsuya, S.; Yokota, Y.; Fujiwara, T.; Mori, N.; Takabe, T.
OsBADH1 is possibly involved in acetaldehyde oxidation in rice plant peroxisomes
FEBS Lett.
583
3625-3629
2009
Oryza sativa
Kovach, M.J.; Calingacion, M.N.; Fitzgerald, M.A.; McCouch, S.R.
The origin and evolution of fragrance in rice (Oryza sativa L.)
Proc. Natl. Acad. Sci. USA
106
14444-14449
2009
Oryza sativa
Kuaprasert, B.; Silprasit, K.; Horata, N.; Khunrae, P.; Wongpanya, R.; Boonyalai, N.; Vanavichit, A.; Choowongkomon, K.
Purification, crystallization and preliminary X-ray analysis of recombinant betaine aldehyde dehydrogenase 2 (OsBADH2), a protein involved in jasmine aroma, from Thai fragrant rice (Oryza sativa L.)
Acta Crystallogr. Sect. F
67
1221-1223
2011
Oryza sativa
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