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Literature summary extracted from

  • Liu, Y.; Song, Y.; Zeng, S.; Patra, B.; Yuan, L.; Wang, Y.
    Isolation and characterization of a salt stress-responsive betaine aldehyde dehydrogenase in Lycium ruthenicum Murr (2018), Physiol. Plant., 163, 73-87 .
    View publication on PubMed

Application

EC Number Application Comment Organism
1.2.1.8 biotechnology overexpression of AMADHs with high BADH activities is an important strategy to genetically engineer Solanaceae crop plants, such as tomato and tobacco, to produe glycine betaine Lycium ruthenicum

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.8 gene AMADH1, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), quantitative real-time PCR enzyme expression analysis Lycium ruthenicum
1.2.1.19 gene AMADH1, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), quantitative real-time PCR enzyme expression analysis Lycium ruthenicum
1.2.1.19 gene AMADH2, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), quantitative real-time PCR enzyme expression analysis Lycium ruthenicum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.8 additional information
-
additional information Michaelis-Menten kinetics, except for LrAMADH1 on 4-aminobutyraldehyde Lycium ruthenicum
1.2.1.8 0.665
-
Betaine aldehyde pH 8.0, 30°C, recombinant isozyme LrAMADH1 Lycium ruthenicum
1.2.1.19 additional information
-
additional information Michaelis-Menten kinetics Lycium ruthenicum
1.2.1.19 additional information
-
additional information Michaelis-Menten kinetics, except for LrAMADH1 on 4-aminobutyraldehyde Lycium ruthenicum
1.2.1.19 0.00394
-
4-Aminobutyraldehyde pH 8.0, 30°C, recombinant isozyme LrAMADH1 Lycium ruthenicum
1.2.1.19 0.0148
-
3-aminopropionaldehyde pH 8.0, 30°C, recombinant isozyme LrAMADH1 Lycium ruthenicum
1.2.1.19 0.0259
-
3-aminopropionaldehyde pH 8.0, 30°C, recombinant isozyme LrAMADH1 Lycium ruthenicum
1.2.1.19 0.0312
-
4-Aminobutyraldehyde pH 8.0, 30°C, recombinant isozyme LrAMADH1 Lycium ruthenicum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.2.1.19 peroxisome
-
Lycium ruthenicum 5777
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.8 betaine aldehyde + NAD+ + H2O Lycium ruthenicum
-
betaine + NADH + 2 H+
-
?
1.2.1.19 3-aminopropionaldehyde + NAD+ + H2O Lycium ruthenicum
-
3-aminopropanoate + NADH + 2 H+
-
?
1.2.1.19 4-aminobutyraldehyde + NAD+ + H2O Lycium ruthenicum
-
4-aminobutanoate + NADH + 2 H+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.8 Lycium ruthenicum A0A1P8VFW6 from Turpan Desert Botanical Garden of the Chinese Academy of Sciences, China
-
1.2.1.8 no activity in Lycium ruthenicum
-
UniProt ID A0A1P8VFW6
-
1.2.1.19 Lycium ruthenicum A0A1P8VFW6 from Turpan Desert Botanical Garden of the Chinese Academy of Sciences, China
-
1.2.1.19 Lycium ruthenicum A0A1P8VFW8 from Turpan Desert Botanical Garden of the Chinese Academy of Sciences, China
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.8 recombinant His-tagged isozyme AMADH1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Lycium ruthenicum
1.2.1.19 recombinant His-tagged isozyme AMADH1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Lycium ruthenicum
1.2.1.19 recombinant His-tagged isozyme AMADH2 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Lycium ruthenicum

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.1.8 fruit
-
Lycium ruthenicum
-
1.2.1.8 additional information tissue specific enzyme expression analysis by quantitative real-time PCR Lycium ruthenicum
-
1.2.1.8 seedling
-
Lycium ruthenicum
-
1.2.1.19 fruit
-
Lycium ruthenicum
-
1.2.1.19 additional information tissue specific enzyme expression analysis by quantitative real-time PCR Lycium ruthenicum
-
1.2.1.19 seedling
-
Lycium ruthenicum
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.8 betaine aldehyde + NAD+ + H2O
-
Lycium ruthenicum betaine + NADH + 2 H+
-
?
1.2.1.8 additional information the enzyme is also active with 4-aminobutyraldehyde and 3-aminopropionaldehyde, EC 1.2.1.19 Lycium ruthenicum ?
-
-
1.2.1.19 3-aminopropionaldehyde + NAD+ + H2O
-
Lycium ruthenicum 3-aminopropanoate + NADH + 2 H+
-
?
1.2.1.19 4-aminobutyraldehyde + NAD+ + H2O
-
Lycium ruthenicum 4-aminobutanoate + NADH + 2 H+
-
?
1.2.1.19 additional information no activity with betaine aldehyde Lycium ruthenicum ?
-
-
1.2.1.19 additional information the enzyme is also active with betaine aldehyde, EC 1.2.1.8 Lycium ruthenicum ?
-
-

Synonyms

EC Number Synonyms Comment Organism
1.2.1.8 AMADH
-
Lycium ruthenicum
1.2.1.8 AMADH1
-
Lycium ruthenicum
1.2.1.8 aminoaldehyde dehydrogenase
-
Lycium ruthenicum
1.2.1.8 BADH
-
Lycium ruthenicum
1.2.1.8 betaine aldehyde dehydrogenase
-
Lycium ruthenicum
1.2.1.8 More see also EC 1.2.1.19 Lycium ruthenicum
1.2.1.19 AMADH
-
Lycium ruthenicum
1.2.1.19 AMADH1
-
Lycium ruthenicum
1.2.1.19 AMADH2
-
Lycium ruthenicum
1.2.1.19 aminoaldehyde dehydrogenase
-
Lycium ruthenicum
1.2.1.19 BADH
-
Lycium ruthenicum
1.2.1.19 betaine aldehyde dehydrogenase
-
Lycium ruthenicum
1.2.1.19 More see also EC 1.2.1.8 Lycium ruthenicum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.8 30
-
assay at Lycium ruthenicum
1.2.1.19 30
-
assay at Lycium ruthenicum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.8 0.004
-
Betaine aldehyde pH 8.0, 30°C, recombinant isozyme LrAMADH1 Lycium ruthenicum
1.2.1.19 1
-
3-aminopropionaldehyde pH 8.0, 30°C, recombinant isozyme LrAMADH1 Lycium ruthenicum
1.2.1.19 1.13
-
4-Aminobutyraldehyde pH 8.0, 30°C, recombinant isozyme LrAMADH1 Lycium ruthenicum
1.2.1.19 1.32
-
4-Aminobutyraldehyde pH 8.0, 30°C, recombinant isozyme LrAMADH1 Lycium ruthenicum
1.2.1.19 2.38
-
3-aminopropionaldehyde pH 8.0, 30°C, recombinant isozyme LrAMADH1 Lycium ruthenicum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.8 8
-
assay at Lycium ruthenicum
1.2.1.19 8
-
assay at Lycium ruthenicum

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.8 NAD+
-
Lycium ruthenicum
1.2.1.19 NAD+
-
Lycium ruthenicum

Expression

EC Number Organism Comment Expression
1.2.1.8 Lycium ruthenicum in NaCl treated seedlings, accompanied by elevated GB accumulation, expression of LrAMADH1 is upregulated, indicating response of LrAMADH1 to salt stress in Lycium ruthenicum up
1.2.1.19 Lycium ruthenicum in NaCl treated seedlings, accompanied by elevated GB accumulation, expression of LrAMADH1 is upregulated, indicating response of LrAMADH1 to salt stress in Lycium ruthenicum up

General Information

EC Number General Information Comment Organism
1.2.1.8 metabolism in higher plants, glycine betaine (GB) is synthesized by two-step oxidation of choline. The first step is catalyzed by ferredoxin-dependent choline monooxygenase (CMO, EC 1.14.15.7) to produce betaine aldehyde (BAL). BAL is converted to GB by aminoaldehyde dehydrogenase (AMADH, EC 1.2.1.19) containing the activities of betaine aldehyde dehydrogenase (BADH) Lycium ruthenicum
1.2.1.8 additional information for Ile445 containing AMADHs, the existence of Asn290 rather than Thr290 leads to detectable BADH activity Lycium ruthenicum
1.2.1.8 physiological function isozyme LrAMADH1 shows low betaine aldehyde dehydrogenase activity, but is proved as bona fide BADH, which involves in glycine betaine (GB) synthesis in planta and responds to salt stress in Lycium ruthenicum plants Lycium ruthenicum
1.2.1.19 metabolism enzyme LrAMADH2 is not involved in glycine betaine biosynthesis Lycium ruthenicum
1.2.1.19 metabolism in higher plants, glycine betaine (GB) is synthesized by two-step oxidation of choline. The first step is catalyzed by ferredoxin-dependent choline monooxygenase (CMO, EC 1.14.15.7) to produce betaine aldehyde (BAL). BAL is converted to GB by aminoaldehyde dehydrogenase (AMADH, EC 1.2.1.19) containing the activities of betaine aldehyde dehydrogenase (BADH) Lycium ruthenicum
1.2.1.19 additional information AMADH2 lacks Ile445, that is contained in all enzymes with BADH activity (EC 1.2.1.8) Lycium ruthenicum
1.2.1.19 additional information for Ile445 containing AMADHs, the existence of Asn290 rather than Thr290 leads to detectable BADH activity Lycium ruthenicum
1.2.1.19 physiological function isozyme LrAMADH1 shows low betaine aldehyde dehydrogenase activity, but is proved as bona fide BADH, which involves in glycine betaine (GB) synthesis in planta and responds to salt stress in Lycium ruthenicum plants Lycium ruthenicum

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.2.1.8 0.006
-
Betaine aldehyde pH 8.0, 30°C, recombinant isozyme LrAMADH1 Lycium ruthenicum
1.2.1.19 42.3
-
4-Aminobutyraldehyde pH 8.0, 30°C, recombinant isozyme LrAMADH1 Lycium ruthenicum
1.2.1.19 67.6
-
3-aminopropionaldehyde pH 8.0, 30°C, recombinant isozyme LrAMADH1 Lycium ruthenicum
1.2.1.19 91.89
-
3-aminopropionaldehyde pH 8.0, 30°C, recombinant isozyme LrAMADH1 Lycium ruthenicum
1.2.1.19 286.8
-
4-Aminobutyraldehyde pH 8.0, 30°C, recombinant isozyme LrAMADH1 Lycium ruthenicum