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Information on EC 1.2.1.8 - betaine-aldehyde dehydrogenase and Organism(s) Spinacia oleracea and UniProt Accession P17202

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IUBMB Comments
In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria. In contrast, different enzymes are involved in the first reaction. In plants, this reaction is catalysed by EC 1.14.15.7 (choline monooxygenase), whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase) . In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase).
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Spinacia oleracea
UNIPROT: P17202
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Word Map
The taxonomic range for the selected organisms is: Spinacia oleracea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
badh2, badh1, pabadh, osbadh2, betaine-aldehyde dehydrogenase, betaine aldehyde dehydrogenase 2, osbadh1, pkbadh, badh2-e7, badh2-e2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
betaine aldehyde dehydrogenase
-
betaine aldehyde dehydrogenase, chloroplastic
-
betaine aldehyde dehydrogenase
betaine aldehyde oxidase
-
-
-
-
dehydrogenase, betaine aldehyde
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -
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 hide
9028-90-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
show the reaction diagram
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
show the reaction diagram
-
-
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
-
-
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 + NADP+ + H2O
betaine + NADPH
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
show the reaction diagram
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
show the reaction diagram
-
-
-
-
ir
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
-
-
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.
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
-
mutant enzyme is less sensitive to inhibition than wild-type enzyme
Betaine aldehyde
-
the enzyme is reversibly and partially inactivated by betaine aldehyde in the absence of NAD+ in a time- and concentration-dependent mode
choline
-
mutant enzyme shows stronger inhibition compared to wild-type enzyme
Isovaleraldehyde
-
wild-type enzyme shows stronger inhibition than the mutant enzyme
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
-
enhances activity
glycine betaine
-
activates the wild-type enzyme but not the mutant enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09 - 1.791
Betaine aldehyde
0.0028 - 0.029
NAD+
0.003 - 0.037
4-Aminobutyraldehyde
0.065 - 0.208
Betaine aldehyde
0.00946 - 0.136
NAD+
0.635
NADP+
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.29 - 3.36
Betaine aldehyde
0.39 - 4.25
NAD+
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.41 - 35
Betaine aldehyde
22 - 243
NAD+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.075
-
BADH I
0.311
-
BADH II
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5 - 9
-
BADH I and BADH II
additional information
-
mutant enzyme E103Q exhibits a broader temperature optimum than the wild-type enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
pH 7.0: about 40% of maximal activity, pH 9.0: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
source for isolating RNA
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
a minor isoenzyme
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
some truncated transcripts of BADH are present in several crops. Such truncated transcripts may cause the accumulation of 2AP (2-acetyl-1-pyrroline), which is a key aroma compound. There is a possibility that inhibition of BADH function produces 2AP-based fragrance in main crops because of the existence of BADH isozymes. But the BADH transcripts from plant species such as Arabidopsis (Arabidopsis thaliana), spinach (Spinacia oleracea) and tomato (Solanum lycopersicum), correctly process the mRNA
physiological function
physiological function
-
expression of the BADH gene in sweet potato increases enzyme activity and glycine betaine in these transgenic sweet potato plants, which subsequently improves their tolerance to multiple abiotic stresses including salt, oxidative stress, and low temperature by induction or activation reactive oxygen species scavenging and the accumulation of proline
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BADH_SPIOL
497
0
54270
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
104000
-
BADH I and BADH II, disc gradient gel electrophoresis
110000
-
gel filtration
120000
-
gel filtration
40000
-
1 * 40000 + 1 * 64000, BADH II, SDS-PAGE
54267
-
x * 54267, calculation from nucleotide sequence
60000
-
2 * 60000, SDS-PAGE
63000
-
2 * 63000, SDS-PAGE
64000
-
1 * 40000 + 1 * 64000, BADH II, SDS-PAGE
98000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 54267, calculation from nucleotide sequence
dimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A441C
the mutant exhibited almost wild type activity with betaine aldehyde
A441F
the mutant shows no activity with betaine aldehyde
A441I
the mutant shows no activity with betaine aldehyde
A441S
the mutant exhibits slightly reduced activity with betaine aldehyde
A441T
the mutant exhibits clearly reduced activity with betaine aldehyde
A441V
the mutant shows no activity with betaine aldehyde
A441C
-
the mutant demonstrates reduced substrate inhibition by betaine aldehyde
A441I
-
the mutant demonstrates reduced substrate inhibition by betaine aldehyde
C450S
-
the mutant is not inhibited by betaine aldehyde
E103K
-
mutant enzyme has no activity with betaine aldehyde and 4-aminobutyraldehyde
E103Q
additional information
transgenic expression of the enzyme in Trachypsermum ammi to reduce salinity and drought stresses results in improved seedling fresh weight, plant height, proline content, relative water content, and secondary metabolites content. Recombinant expression in Nicotiana tabacum and Solanum lycopersicum to reduce temperature stress results in improved PSII efficiency, chlorophyll fluorescence, induction kinetics, activity of CAT, SOD and APX, and ascorbate and glutathione contents in tobacco, as well as in improved lipid peroxidation, glycine betaine accumulation, PSII photochemical activity, hydrogen peroxide and superoxide anion radical levels, CO2 assimilation, PSII photochemical activity, hydrogen peroxide, and superoxide anion radical and MDA levels in tomato. Recombinant expression in transgenic walnut plants to reduce drought and salinity stresses results in improved shoot height and survival rate
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 11
-
mutant enzyme is less stable than the wild-type enzyme in the pH-range 5-11
655947
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
120 min, about 80% decrease of activity
50
-
120 min, complete inactivation
additional information
-
mutant enzyme E103Q appears to be more heat labile than the wild-type enzyme. Mutant enzyme E103Q and wild-type enzyme are protected by NAD+ against thermal inactivation in a similar manner. Neither glycine betaine nor NaCl can afford protection against thermal inactivation in the mutant enzyme whereas some protection is observed in the wild-type enzyme
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, less than 30% loss of activity after 18 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2 enzyme forms: BADH I and BADH II
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene BADH, Agrobacterium tumefaciens-mediated recombinant expression in Trachyspermum ammi, Nicotiana tabacum, and Solanum lycopersicum, as well as in Juglans regia
gene BADH, sequence comparisons
To compare the posttranscriptional processing patterns of the BADH homologs between cereal crop species and more distantly related dicotyledonous species, RT-PCR experiments using total RNA extracted from seedlings of spinach are conducted. Primers designed to amplify the full length of mRNA of BADH homologs are used. As anticipated, the RT-PCR products of BADH homologs from spinach are of expected size for correctly processed transcripts. Sequencing analysis of 4 cDNA clones confirms the correct processing.
expressed in Ipomoea batatas cultivar Sushu-2 via Agrobacterium-mediated transformation
-
in Nicotiana tabacum, the BADH gene isolating from spinach is used to construct a vector plasmid that contained the promoter for 35S ribosomal RNA from CaMV35S, the sequence encoding the transit peptide of the small subunit of Rubisco of tobacco and the terminator of the gene for nopaline synthase. Nicotiana tabacum (wild type K326) is transformed with the resultant plasmid by the standard Agrobacterium-mediated method and five independent lines of transgenic tobacco plants are established. Transformed plants are used as the source of plant materials. The role of glycine betaine in vivo in protecting photosynthesis from salt stress is investigated.
-
mutant enzyme E103Q expressed in Escherichia coli
-
of genes encoding five forms of spinach enzyme: full length, mature, mutant E103Q, mutant E103K and chimera
-
overexpression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molecular biology
BADH application as a marker for chloroplast engineering without using antibiotic can avoid transferring antibiotic genes from the plant and thus assists to allay public concern regarding genetic modifications
agriculture
-
potential application, genetic engineering results in enhanced tolerance of growth of young seedlings to salt stress. Results of investigation shows that transformation with the BADH gene may benefit efforts to improve crop yields in saline, arid and semi-arid regions where plants suffer salt stress
additional information
BADH isolated from spinach is successfully utilised for selection of chloroplast transformation of tobacco in order to prevent the risk of transferring antibiotic resistance genes to gut microbes or the environment
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Weretilnyk, E.A.; Hanson, A.D.
Molecular cloning of a plant betaine-aldehyde dehydrogenase, an enzyme implicated in adaptation to salinity and drought
Proc. Natl. Acad. Sci. USA
87
2745-2749
1990
Spinacia oleracea
Manually annotated by BRENDA team
Weretilnyk, E.A.; Bednarek, S.; McCue, K.F.; Rhodes, D.; Hanson, A.D.
Comparative biochemical and immunological studies of the glycine betaine synthesis pathway in diverse families of dicotyledons
Planta
178
342-352
1989
Amaranthus caudatus, Convolvulus arvensis, Helianthus annuus, Lycium ferocissimum, Portulaca oleracea, Solanum lycopersicum, Spinacia oleracea
Manually annotated by BRENDA team
Weretilnyk, E.A.; Hanson, A.D.
Betaine aldehyde dehydrogenase from spinach leaves: purification, in vitro translation of the mRNA, and regulation by salinity
Arch. Biochem. Biophys.
271
56-63
1989
Spinacia oleracea
Manually annotated by BRENDA team
Pan, S.M.
Betaine aldehyde dehydrogenase in spinach
Bot. Bull. Acad. Sin.
29
255-263
1988
Spinacia oleracea
-
Manually annotated by BRENDA team
Arakawa, K.; Takabe, T.; Sugiyama, T.; Akazawa, T.
Purification of betaine-aldehyde dehydrogenase from spinach leaves and preparation of its antibody
J. Biochem.
101
1485-1488
1987
Spinacia oleracea
Manually annotated by BRENDA team
Weigel, P.; Weretilnyk, A.E.; Hanson, A.D.
Betaine aldehyde oxidation by spinach chloroplasts
Plant Physiol.
82
753-759
1986
Spinacia oleracea
Manually annotated by BRENDA team
Pan, S.M.; Moreau, R.A.; Yu, C.; Huang, A.H.C.
Betaine accumulation and betaine-aldehyde dehydrogenase in spinach leaves
Plant Physiol.
67
1105-1108
1981
Kandelia candel, Spinacia oleracea
Manually annotated by BRENDA team
Hibino, T.; Meng, Y.L.; Kawamitsu, Y.; Uehara, N.; Matsuda, N.; Tanaka, Y.; Ishikawa, H.; Baba, S.; Takabe, T.; Wada, K.; Ishii, T.
Molecular cloning and functional characterization of two kinds of betaine-aldehyde dehydrogenase in betaine-accumulating mangrove Avicennia marina (Forsk.) Vierh
Plant Mol. Biol.
45
353-363
2001
Avicennia marina, Bruguiera gymnorhiza, Escherichia coli, Rhizophora stylosa, Spinacia oleracea
Manually annotated by BRENDA team
Incharoensakdi, A.; Matsuda, N.; Hibino, T.; Meng, Y.L.; Ishikawa, H.; Hara, A.; Funaguma, T.; Takabe, T.; Takabe, T.
Overproduction of spinach betaine aldehyde dehydrogenase in Escherichia coli. Structural and functional properties of wild-type, mutants and E. coli enzymes
Eur. J. Biochem.
267
7015-7023
2000
Spinacia oleracea
Manually annotated by BRENDA team
Incharoensakdi, A.; Hibino, T.; Takabe, T.
Glu103Gln site-directed mutation causes an alteration in physical properties of spinach betaine aldehyde dehydrogenase
J. Biochem. Mol. Biol. Biophys.
6
243-248
2002
Spinacia oleracea
Manually annotated by BRENDA team
Yang, X.; Liang, Z.; Wen, X.; Lu, C.
Genetic engineering of the biosynthesis of glycinebetaine leads to increased tolerance of photosynthesis to salt stress in transgenic tobacco plants
Plant Mol. Biol.
66
73-86
2008
Spinacia oleracea
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Fan, W.; Zhang, M.; Zhang, H.; Zhang, P.
Improved tolerance to various abiotic stresses in transgenic sweet potato (Ipomoea batatas) expressing spinach betaine aldehyde dehydrogenase
PLoS ONE
7
e37344
2012
Spinacia oleracea
Manually annotated by BRENDA team
Zarate-Romero, A.; Murillo-Melo, D.S.; Mujica-Jimenez, C.; Montiel, C.; Munoz-Clares, R.A.
Reversible, partial inactivation of plant betaine aldehyde dehydrogenase by betaine aldehyde: mechanism and possible physiological implications
Biochem. J.
473
873-885
2016
Spinacia oleracea
Manually annotated by BRENDA team
Munoz-Clares, R.A.; Riveros-Rosas, H.; Garza-Ramos, G.; Gonzalez-Segura, L.; Mujica-Jimenez, C.; Julian-Sanchez, A.
Exploring the evolutionary route of the acquisition of betaine aldehyde dehydrogenase activity by plant ALDH10 enzymes: implications for the synthesis of the osmoprotectant glycine betaine
BMC Plant Biol.
14
149
2014
Spinacia oleracea (P17202)
Manually annotated by BRENDA team
Golestan Hashemi, F.; Ismail, M.; Rafii, M.; Aslani, F.; Miah, G.; Muharam, F.
Critical multifunctional role of the betaine aldehyde dehydrogenase gene in plants
Biotechnol. Biotechnol. Equip.
32
815-829
2018
Ammopiptanthus nanus, Arabidopsis thaliana (Q9S795), Arabidopsis thaliana (Q9STS1), Glycine max (B0M1A6), Hordeum vulgare subsp. vulgare (A4UUF3), Madhuca longifolia var. latifolia, Oryza sativa Japonica Group (O24174), Oryza sativa Japonica Group (Q84LK3), Pandanus amaryllifolius (A0A2Z2GYT8), Solanum lycopersicum, Spinacia oleracea (P17202), Triticum aestivum (Q8LGQ9), Vallaris sp., Zea mays (Q53CF4)
-
Manually annotated by BRENDA team
Niazian, M.; Sadat-Noori, S.A.; Tohidfar, M.; Mortazavian, S.M.M.; Sabbatini, P.
Betaine aldehyde dehydrogenase (BADH) vs. flavodoxin (Fld) two important genes for enhancing plants stress tolerance and productivity
Front. Plant Sci.
12
650215
2021
Ammopiptanthus nanus, Atriplex canescens (S4S7H4), Atriplex hortensis (P42757), Hordeum vulgare (Q40024), Spinacia oleracea (P17202), Suaeda liaotungensis (Q8W5A1), Triticum aestivum (Q8LGQ9)
Manually annotated by BRENDA team