1.2.1.8: betaine-aldehyde dehydrogenase
This is an abbreviated version!
For detailed information about betaine-aldehyde dehydrogenase, go to the full flat file.
Word Map on EC 1.2.1.8
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1.2.1.8
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badhs
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aroma
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fragrant
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2-acetyl-1-pyrroline
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osmoprotectant
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molecular biology
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basmati
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non-fragrant
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scent
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4-aminobutyraldehyde
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medicine
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3-aminopropionaldehyde
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non-aromatic
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aminoaldehyde
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jasmine
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agriculture
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biotechnology
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energy production
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food industry
- 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
Reaction
Synonyms
AcBADH, ALD10, aldehyde dehydrogenase, ALDH10, ALDH10A8, ALDH10A9, AMADH, AMADH1, aminoaldehyde dehydrogenase, BADH, BADH1, BADH2, badh2-E2, badh2-E7, betaine aldehyde dehydrogenase, betaine aldehyde dehydrogenase 1, betaine aldehyde dehydrogenase 1, chloroplastic, betaine aldehyde dehydrogenase 2, betaine aldehyde dehydrogenase, chloroplastic, betaine aldehyde oxidase, betaine aldehyde: NAD(P)+ oxidoreductase, betaine aldehyde: NAD+ oxidoreductase, betaine aldehyde:NAD(P)+ oxidoreductase, betaine aldehyde:NAD+ oxidoreductase, betaine-aldehyde dehydrogenase, BetB, dehydrogenase, betaine aldehyde, JcBD1, LcBADH, More, OsALDH10-1, OsALDH10-2, OsBADH1, OsBADH2, PaBADH, PaBADH2, pkBADH, PND BADH2, SACOL2628, YdcW, ZBD1, Zoysia betaine aldehyde dehydrogenase 1
ECTree
1.2.1.8 betaine-aldehyde dehydrogenaseAdvanced search results
results (
results (Specific Activity
Specific Activity on EC 1.2.1.8 - betaine-aldehyde dehydrogenase
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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
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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
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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
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quantification of 2-acetyl-1-pyrroline (2AP) and other metabolites in vivo
