Information on EC 1.2.1.8 - betaine-aldehyde dehydrogenase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.2.1.8
-
RECOMMENDED NAME
GeneOntology No.
betaine-aldehyde dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
show the reaction diagram
ping-pong mechanism
-
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
show the reaction diagram
iso-ordered bi-bi steady state mechanism
-
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
show the reaction diagram
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+
show the reaction diagram
iso random steady state mechanism
-
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
show the reaction diagram
steady-state ordered bi bi or rapid equilibrium mechanism
-
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
show the reaction diagram
steady-state ordered mechanism, in which NAD+ binds first and NADH leaves last
-
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
show the reaction diagram
catalyzes the last irreversible step in the synthesis of the osmoprotector glycine betaine
-
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
show the reaction diagram
catalyzes the last step of the two-step oxidation
-
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
show the reaction diagram
the enzyme catalyzes the second step of the two-step conversion of choline into glycine betaine
O24174, Q06DE4
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
show the reaction diagram
ping-pong mechanism
Cylindrocarpon didymum M-1
-
-
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidation
Q155V4, -
-
oxidation
-
-
oxidation
-
-
oxidation
-
-
oxidation
B2BBY6
-
oxidation
O24174, Q06DE4
;
oxidation
-
-
oxidation
-
-
oxidation
-
-
redox reaction
-
-
-
-
redox reaction
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
choline degradation I
-
glycine betaine biosynthesis I (Gram-negative bacteria)
-
glycine betaine biosynthesis II (Gram-positive bacteria)
-
glycine betaine biosynthesis III (plants)
-
Glycine, serine and threonine metabolism
-
Metabolic 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).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aldehyde dehydrogenase
Q9HTJ1
-
ALDH10A8
Q9S795
gene name
ALDH10A9
Q9STS1
gene name
BADH
-
-
-
-
BADH
Q9S795, Q9STS1
-
BADH
-
-
BADH
Q94IC0, Q94IC1
-
BADH
B2BBY6
-
BADH
O24174
-
BADH
O24174
former name
BADH
Q06DE4
-
BADH
P17202
-
BADH
Q155V4
-
BADH
-, Q8LGQ9
-
BADH
Q53CF4
-
BADH
Q6BD86, Q6BD88, Q6BD90, Q6BD91, Q6BD93, Q6BD95, Q6BD99, Q6BDA3, Q6BDA4
-
BADH1
Q9S795
-
BADH1
Q94IC0
-
BADH1
-
-
BADH1
-
isozyme
BADH1
Q53CF4
-
BADH2
Q9STS1
-
BADH2
Q94IC1
-
BADH2
-
isozyme
BADH2
B3VMC0
-
BADH2
Q8LGQ9
-
BADH2
Q53CF4
-
badh2-E2
B3VMC1
recessive allele, truncated form, with a 7-bp deletion in exon 2 (82 residues)
badh2-E7
B3VMC2
recessive allele, truncated form (251 amino acid polypeptide)
betaine aldehyde dehydrogenase
-
-
-
-
betaine aldehyde dehydrogenase
Q9S795, Q9STS1
-
betaine aldehyde dehydrogenase
-
-
betaine aldehyde dehydrogenase
-
-
betaine aldehyde dehydrogenase
-
-
betaine aldehyde dehydrogenase
-
-
betaine aldehyde dehydrogenase
Q94IC0, Q94IC1
-
betaine aldehyde dehydrogenase
B2BBY6
-
betaine aldehyde dehydrogenase
-
-
betaine aldehyde dehydrogenase
-
-
betaine aldehyde dehydrogenase
B3VMC0
-
betaine aldehyde dehydrogenase
O24174, Q06DE4
-
betaine aldehyde dehydrogenase
-
-
betaine aldehyde dehydrogenase
-
-
betaine aldehyde dehydrogenase
Q9HTJ1
-
betaine aldehyde dehydrogenase
-
-
betaine aldehyde dehydrogenase
-
-
betaine aldehyde dehydrogenase
P17202
-
betaine aldehyde dehydrogenase
-
-
betaine aldehyde dehydrogenase
Q155V4
-
betaine aldehyde dehydrogenase
-
-
betaine aldehyde dehydrogenase
-, Q8LGQ9
-
betaine aldehyde dehydrogenase
Q53CF4
-
betaine aldehyde dehydrogenase
-
-
betaine aldehyde dehydrogenase
Q6BD86, Q6BD88, Q6BD90, Q6BD91, Q6BD93, Q6BD95, Q6BD99, Q6BDA3, Q6BDA4
-
betaine aldehyde dehydrogenase 1
-
-
betaine aldehyde dehydrogenase 1, chloroplastic
Q9S795
-
betaine aldehyde dehydrogenase 2
Q9STS1
-
betaine aldehyde dehydrogenase 2
-
-
betaine aldehyde dehydrogenase, chloroplastic
P17202
-
betaine aldehyde oxidase
-
-
-
-
betaine aldehyde: NAD(P)+ oxidoreductase
-
-
betaine aldehyde: NAD+ oxidoreductase
-
-
betaine aldehyde:NAD(P)+ oxidoreductase
-
-
betaine aldehyde:NAD(P)+ oxidoreductase
-
-
betaine aldehyde:NAD(P)+ oxidoreductase
Q9HTJ1
-
betaine aldehyde:NAD+ oxidoreductase
-
-
betaine-aldehyde dehydrogenase
Q9HTJ1
-
dehydrogenase, betaine aldehyde
-
-
-
-
JcBD1
B2BBY6
-
OsALDH10-1
O24174
-
OsALDH10-2
Q06DE4
-
OsBADH1
O24174
-
OsBADH2
Q06DE4
-
PaBADH
Q9HTJ1
-
pkBADH
-
-
ZBD1
Q6BD86, Q6BD88, Q6BD90, Q6BD91, Q6BD93, Q6BD95, Q6BD99, Q6BDA3, Q6BDA4
-
Zoysia betaine aldehyde dehydrogenase 1
Q6BD86, Q6BD88, Q6BD90, Q6BD91, Q6BD93, Q6BD95, Q6BD99, Q6BDA3, Q6BDA4
-
CAS REGISTRY NUMBER
COMMENTARY
9028-90-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Amaranthus sp.
-
-
-
Manually annotated by BRENDA team
ecotype Col-0
UniProt
Manually annotated by BRENDA team
five transgenic tomato (Lycopersicon esculentum Mill) lines T3-1, T3-3, T3-5, T3-8 and T3-9 with BADH gene from Atriplex hortensis are analysed concerning their behaviour under salt stress conditions and compared with cv. Bailichun wild type
-
-
Manually annotated by BRENDA team
Cylindrocarpon didymum M-1
M-1
-
-
Manually annotated by BRENDA team
over-producing strain carrying the structural gene for the enzyme on the plasmid pBR322
-
-
Manually annotated by BRENDA team
aldehyde dehydrogenase E3 isoenzyme is a betaine aldehyde dehydrogenase
-
-
Manually annotated by BRENDA team
commentary
UniProt
Manually annotated by BRENDA team
cultivars Japonica and Indica
-
-
Manually annotated by BRENDA team
subspecies japonica and indica
UniProt
Manually annotated by BRENDA team
susp. japonica; susp. japonica and indica; different varieties are investigated
Uniprot
Manually annotated by BRENDA team
Thai fragrant rice
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa A-16
A-16
-
-
Manually annotated by BRENDA team
2 enzyme forms: BADG I and BADH II. BADH II comprises more than 60% of the total activity
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
positive clone isolated after a cDNA library screening coding for a betaine aldehyde dehydrogenase isozyme
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
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
-
the badh2 gene alone is not sufficient enough to explain the genetic and molecular basis of fragrance in rice
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
-
overexpression of the betaine aldehyde dehydrogenase gene in transgenic trifoliate orange enhances salt stress tolerance and leads to accumulation of higher levels of glycine betaine
physiological function
Q153G6
the enzyme plays a role in salt (400 mM NaCl) and other osmotic stresses tolerance
physiological function
-, Q9S795, Q9STS1
ALDH10A8 serves as detoxification enzyme controlling the level of aminoaldehydes, which are produced in cellular metabolism under stress conditions; LDH10A9 serves as detoxification enzymes controlling the level of aminoaldehydes, which are produced in cellular metabolism under stress conditions
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,3-diaminopropane + NAD+ + H2O
?
show the reaction diagram
-
-
-
-
?
3-aminopropionaldehyde + NAD(P)+ + H2O
?
show the reaction diagram
-
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
show the reaction diagram
-
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
show the reaction diagram
B3VMC0, B3VMC1, B3VMC2, -
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
show the reaction diagram
-, Q9S795, Q9STS1
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionic acid + NADH + H+
show the reaction diagram
Q6BD86, Q6BD88, Q6BD90, Q6BD91, Q6BD93, Q6BD95, Q6BD99, Q6BDA3, Q6BDA4, -
-
-
-
-
3-aminopropionaldehyde + NAD+ + H2O
?
show the reaction diagram
-
-
-
-
?
3-dimethylsulfoniopropionaldehyde + NAD(P)+ + H2O
?
show the reaction diagram
-
-
-
-
?
3-dimethylsulfoniopropionaldehyde + NAD+ + H2O
?
show the reaction diagram
-
-
-
-
?
3-dimethylsulfoniopropionaldehyde + NAD+ + O2
3-dimethylsulfoniopropionate + NADH
show the reaction diagram
-
steady state bi bi mechanism with ordered addition of substrates and random release of products
-
-
ir
3-N-trimethylaminopropionaldehyde + NAD+ + H2O
?
show the reaction diagram
-
-
-
-
?
3-N-trimethylaminopropionaldehyde + NAD+ + H2O
3-N-trimethylaminopropionate + NADH + H+
show the reaction diagram
-
-
-
-
?
4-aminobutylaldehyde + NAD+ + H2O
4-aminobutyrate + NADH
show the reaction diagram
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
show the reaction diagram
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
show the reaction diagram
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
show the reaction diagram
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
show the reaction diagram
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
show the reaction diagram
-
no activity
-
-
-
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
show the reaction diagram
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
show the reaction diagram
Q6BD86, Q6BD88, Q6BD90, Q6BD91, Q6BD93, Q6BD95, Q6BD99, Q6BDA3, Q6BDA4, -
-
-
-
-
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
show the reaction diagram
-, Q9S795, Q9STS1
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH + H+
show the reaction diagram
B3VMC0, B3VMC1, B3VMC2, -
-
-
-
?
4-gamma-aminobutyraldehyde + NAD+ + H2O
?
show the reaction diagram
-
-
-
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutyrate + NADH + H+
show the reaction diagram
-
-
-
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
?
show the reaction diagram
-
-
-
-
?
4-N-trimethylaminobutyraldehyde + NAD(P)+ + H2O
?
show the reaction diagram
-
-
-
-
?
4-N-trimethylaminobutyraldehyde + NAD+ + H2O
?
show the reaction diagram
-
-
-
-
?
4-N-trimethylaminobutyraldehyde + NAD+ + H2O
4-N-trimethylaminobutyrate + NADH + H+
show the reaction diagram
-
-
-
-
?
4-trimethylaminobutyraldehyde + NAD+ + H2O
3-trimethylaminobutyrate + NADH
show the reaction diagram
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
at 20% of the activity with betaine aldehyde
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
show the reaction diagram
-
-
-
-
?
aminoacetaldehyde + NAD+ + H2O
aminoacetate + NADH + H+
show the reaction diagram
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
show the reaction diagram
-
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + 2 H+
show the reaction diagram
-
-
-
-
n
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
show the reaction diagram
-
-
-
-
ir
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
show the reaction diagram
-
-
-
-
ir
betaine aldehyde + NAD(P)+ + H2O
betaine + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
Amaranthus sp.
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
-
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
reverse reaction not detected
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
preferentially uses NADP+ over NAD+
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
equilibrium of the reaction strongly favours betaine formation
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
highly specific for betaine aldehyde
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
enzyme is induced several-fold by salinization
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
enzyme is induced several-fold by salinization
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme is involved in the metabolism of choline, induced during growth on choline
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
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
show the reaction diagram
-
inducible enzyme accumulates in the presence of choline, acetylcholine or betaine in the medium
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
enzyme of the osmoregulatory choline-glycine betaine pathway
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
the age-related acceleration in conversion of choline into betaine probably tends to diminish unesterified choline concentrations
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
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
show the reaction diagram
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
last step in betaine synthesis, a nontoxic or protective osmolyte under saline or dry conditions
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
enzyme catalyzes the final irreversible step in the synthesis of glycine betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-, the enzyme is involved in the metabolism of choline, induced during growth on choline
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
Cylindrocarpon didymum M-1
-
-, synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
Pseudomonas aeruginosa A-16
-
reverse reaction not detected
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
Pseudomonas aeruginosa A-16
-
inducible enzyme accumulates in the presence of choline, acetylcholine or betaine in the medium
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
show the reaction diagram
-
-
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
show the reaction diagram
-, Q9S795, Q9STS1
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
show the reaction diagram
-
-
regulates osmotic pressure and protects enzyme activities; the transgenic plants have a higher accumulation of betaine
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
show the reaction diagram
-
the enzyme catalyzes the second step in the synthesis of the osmoprotectant glycine betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
show the reaction diagram
-
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+
show the reaction diagram
-
more active on medium-chain aldehydes than on betaine aldehyde
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
show the reaction diagram
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 + 2 H+
show the reaction diagram
-, Q9HTJ1
-
-
-
n
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
Q6BD86, Q6BD88, Q6BD90, Q6BD91, Q6BD93, Q6BD95, Q6BD99, Q6BDA3, Q6BDA4, -
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
P17202
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
Q9S795, Q9STS1
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
-
-
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+
show the reaction diagram
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+
show the reaction diagram
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+
show the reaction diagram
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+
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 + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
O24174, Q06DE4
-
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+
show the reaction diagram
O24174, Q06DE4
-
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+
show the reaction diagram
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
betaine + NADH + 2 H+
show the reaction diagram
-
-
accumulation of betaine is a strategy of plants to survive drought, salinity, and extreme temperatures
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NAPH + H+
show the reaction diagram
-
-
-
-
ir
betaine aldehyde + NAD+ H2O
betaine + NADH + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ H2O
betaine + NADH + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ H2O
glycine betaine + NADH + H+
show the reaction diagram
Q153G6
-
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADH
show the reaction diagram
-
no activity with NAD+
-
-
-
betaine aldehyde + NADP+ + H2O
betaine + NADH
show the reaction diagram
-
no activity with NAD+
-
-
-
betaine aldehyde + NADP+ + H2O
betaine + NADH
show the reaction diagram
-
preferentially uses NADP+ over NAD+
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADH
show the reaction diagram
-
75% of the activity with NAD+
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADH
show the reaction diagram
-
25% of the maximal activity with NAD+
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADH
show the reaction diagram
-
NAD+ is preferred over NADP+
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
show the reaction diagram
-
-
-
-
-
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
show the reaction diagram
-
-
-
-
ir
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
show the reaction diagram
-
more active on medium-chain aldehydes than on betaine aldehyde
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
show the reaction diagram
-
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
glycine betaine + NADPH + H+
show the reaction diagram
-
-
-
-
ir
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
show the reaction diagram
-
-
-
-
?
butyraldehyde + NAD+ + H2O
butyrate + NADH
show the reaction diagram
-
at 40% of the activity with betaine aldehyde
-
-
?
butyraldehyde + NADP+ + H2O
butyrate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D,L-glyceraldehyde + NAD+ + H2O
glycerate + NADH + H+
show the reaction diagram
-
-
-
-
?
D,L-glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
show the reaction diagram
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
show the reaction diagram
-
-
-
-
?
formaldehyde + NADP+ + H2O
formate + NADPH + H+
show the reaction diagram
-
-
-
-
?
gamma-aminobutyraldehyde + NAD(P)+ + H2O
?
show the reaction diagram
-
-
-
-
?
glyceraldehyde + NAD+ + H2O
glycerate + NADH
show the reaction diagram
-
at 30% of the activity with betaine aldehyde
-
-
?
glycine betaine aldehyde + NAD+ + H2O
glycine betaine + NADH
show the reaction diagram
-
-
-
-
?
glycine betaine aldehyde + NADP+ + H2O
glycine betaine + NADH
show the reaction diagram
-
-
-
-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH
show the reaction diagram
-
-
-
-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH
show the reaction diagram
-
-
-
-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH + H+
show the reaction diagram
-
-
-
-
?
glycolaldehyde + NADP+ + H2O
glycolate + NADPH + H+
show the reaction diagram
-
-
-
-
?
isovaleraldehyde + NAD+ + H2O
isovalerate + NADH + H+
show the reaction diagram
-
-
-
-
?
isovaleraldehyde + NADP+ + H2O
isovalerate + NADPH + H+
show the reaction diagram
-
-
-
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
?
N-acetyl-4-aminobutyraldehyde + NAD+ + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoate + NADH + H+
show the reaction diagram
-
-
-
-
?
p-nitrobenzaldehyde + NADP+ + H2O
p-nitrobenzoate + NADPH + H+
show the reaction diagram
-
-
-
-
?
phenyl acetaldehyde + NAD+ + H2O
phenyl acetate + NADH + H+
show the reaction diagram
-
-
-
-
?
phenyl acetaldehyde + NADP+ + H2O
phenyl acetate + NADPH + H+
show the reaction diagram
-
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
show the reaction diagram
-
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH
show the reaction diagram
-
-
-
-
?
propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
show the reaction diagram
-
-
-
-
?
undecanal + NAD+ + H2O
undecanoate + NADH + H+
show the reaction diagram
-
-
-
-
?
undecanal + NADP+ + H2O
undecanoate + NADPH + H+
show the reaction diagram
-
-
-
-
?
valeraldehyde + NAD+ + H2O
valerate + NADH + H+
show the reaction diagram
-
-
-
-
?
valeraldehyde + NADP+ + H2O
valerate + NADPH + H+
show the reaction diagram
-
-
-
-
?
methylglyoxal + NADP+ + H2O
? + NADPH + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
no activity with 3-dimethylsulfoniopropionaldehyde
-
-
-
additional information
?
-
-
betaine aldehyde dehydrogenase gene expression in leaves increases with salt stress
-
-
-
additional information
?
-
-
no activity with succinic semialdehyde
-
-
-
additional information
?
-
B3VMC0, B3VMC1, 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, B3VMC1, 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, B3VMC1, 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, Q06DE4
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
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
?
-
-
various other C3-C6 amino acids
-
-
-
additional information
?
-
-
isozyme BADH1 catalyzes the oxidation of acetaldehyde efficiently, while the activity of isozyme BADH2 is extremely low
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
show the reaction diagram
B3VMC0, B3VMC1, B3VMC2, -
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
show the reaction diagram
-, Q9S795, Q9STS1
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
show the reaction diagram
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
show the reaction diagram
-, Q9S795, Q9STS1
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH + H+
show the reaction diagram
B3VMC0, B3VMC1, B3VMC2, -
-
-
-
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + 2 H+
show the reaction diagram
-
-
-
-
n
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
show the reaction diagram
-
-
-
-
ir
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
show the reaction diagram
-
-
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
enzyme is induced several-fold by salinization
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
enzyme is induced several-fold by salinization
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme is involved in the metabolism of choline, induced during growth on choline
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
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
show the reaction diagram
-
inducible enzyme accumulates in the presence of choline, acetylcholine or betaine in the medium
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
enzyme of the osmoregulatory choline-glycine betaine pathway
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
the age-related acceleration in conversion of choline into betaine probably tends to diminish unesterified choline concentrations
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
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
show the reaction diagram
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
last step in betaine synthesis, a nontoxic or protective osmolyte under saline or dry conditions
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
enzyme catalyzes the final irreversible step in the synthesis of glycine betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
show the reaction diagram
-, Q9S795, Q9STS1
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
show the reaction diagram
-
-
regulates osmotic pressure and protects enzyme activities; the transgenic plants have a higher accumulation of betaine
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
show the reaction diagram
-
the enzyme catalyzes the second step in the synthesis of the osmoprotectant glycine betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
show the reaction diagram
-
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+
show the reaction diagram
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 + 2 H+
show the reaction diagram
-, Q9HTJ1
-
-
-
n
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
Q6BD86, Q6BD88, Q6BD90, Q6BD91, Q6BD93, Q6BD95, Q6BD99, Q6BDA3, Q6BDA4, -
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
P17202
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
Q9S795, Q9STS1
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
-
-
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+
show the reaction diagram
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+
show the reaction diagram
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+
show the reaction diagram
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+
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 + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
O24174, Q06DE4
-
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+
show the reaction diagram
O24174, Q06DE4
-
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+
show the reaction diagram
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
betaine + NADH + 2 H+
show the reaction diagram
-
-
accumulation of betaine is a strategy of plants to survive drought, salinity, and extreme temperatures
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NAPH + H+
show the reaction diagram
-
-
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
the enzyme is involved in the metabolism of choline, induced during growth on choline
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
Cylindrocarpon didymum M-1
-
synthesis of betaine
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
Pseudomonas aeruginosa A-16
-
inducible enzyme accumulates in the presence of choline, acetylcholine or betaine in the medium
-
-
?
betaine aldehyde + NAD+ H2O
betaine + NADH + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ H2O
glycine betaine + NADH + H+
show the reaction diagram
Q153G6
-
-
-
?
betaine aldehyde + NADP+ + H2O
glycine betaine + NADPH + H+
show the reaction diagram
-
-
-
-
ir
additional information
?
-
-
betaine aldehyde dehydrogenase gene expression in leaves increases with salt stress
-
-
-
additional information
?
-
B3VMC0, B3VMC1, 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, B3VMC1, 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, B3VMC1, 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, Q06DE4
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD+
-
NAD+ is preferred over NADP+
NAD+
-
NAD+ is preferred over NADP+
NAD+
-
much better affinity for NAD+ than for NADP+
NAD+
Q155V4, -
-
NAD+
-
protective effects of NAD+ against inactivation of BADH by disulfiram
NAD+
B3VMC0, B3VMC1, B3VMC2
; 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+
-
PaBADH uses NAD+ and NADP+ with similar efficiencies
NAD+
O24174, Q06DE4
;
NAD+
-
BADH uses NAD+ with the same efficiency as NADP+; PaBADH uses NADP+ with the same efficiency as NAD+
NAD+
-
the enzyme can use NADP+ with similar efficiency to NAD+
NAD+
-, Q9S795, Q9STS1
;
NADP+
-
NAD+ is preferred over NADP+
NADP+
-
75% of the activity with NAD+
NADP+
-
preferentially uses NADP+ over NAD+
NADP+
-
NAD+ is preferred over NADP+
NADP+
-
much better affinity for NAD+ than for NADP+
NADP+
-
PaBADH uses NAD+ and NADP+ with similar efficiencies
NADP+
O24174, Q06DE4
;
NADP+
-
BADH uses NADP+ with the same efficiency as NAD+; PaBADH uses NADP+ with the same efficiency as NAD+
NADP+
-
the enzyme can use NADP+ with similar efficiency to NAD+
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
increase of concentration from 0 to 0.00075 mM produces a 2fold increase in activity
Ca2+
-
results indicate that transgenic plants have a higher Ca2+ accumulation than the wild type under saline conditions
Cl-
-
treatment of seedlings after germinating with 6.25-200 mmol/l
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+
-
activation up to 0.15 M, decreases activity at higher concentrations
K+
-
stimulates
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+
-
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
K+
-
results indicate that transgenic plants have a higher K+ accumulation than the wild type under saline conditions
K+
-
; the enzyme requires K+ ions for stability and possesses two K+ binding sites per subunit
Na+
-
slight activation up to about 0.3 M
Na+
-
can mimic the effect of K+
Na+
-
treatment of seedlings after germinating with 18.75-400 mmol/l
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
NH4+
-
can mimic the effect of K+
Mg2+
-
0.2 M, slight activation
additional information
-
high salt tolerance: 50% or more of its maximal activity is preserved at 1.0 M Na+ or K+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
-
mutant enzyme is less sensitive to inhibition than wild-type enzyme
1,10-phenanthroline
-
-
1,10-phenanthroline
-
no inhibition at 1 mM
2,2'-dipyridyl
-
no inhibition at 3 mM
3-dimethylsulfoniopropionaldehyde
-
at high concentrations
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
acetaldehyde
-
100 mM, 83% inhibition
acetaldehyde
-
10 mM, 69% inhibition
acetaldehyde
-
-
Acetylcholine
-
10 mM, 18% inhibition
AgNO3
-
3 mM, 90-100% inhibition
AMP
-
competitive with respect to NAD+ and mixed with betaine aldehyde
AMP
-
competitive with respect to NAD+ and mixed with betaine aldehyde and uncompetitive with respect to NAD+
benzaldehyde
-
1 mM, 51% inhibition
benzyltrimethylamine iodide
-
10 mM, 45% inhibition
betaine
-
10 mM, 14% inhibition
betaine
-
product inhibition
Betaine aldehyde
-
above 0.5 mM
Betaine aldehyde
-
substrate inhibition
Betaine aldehyde
-
-
Betaine aldehyde
-
0.5 mM, non-competitive inhibitor against NAD+
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
Butyrylcholine
-
100 mM, 73% inhibition
Ca2+
-
500 mM CaCl2, about 50% loss of activity
Ca2+
-
10 mM CaCl2, 90% inhibition
Ca2+
-
500 mM CaCl2, about 50% loss of activity
Ca2+
-
above 0.00075 mM
choline
-
100 mM, 78% inhibition
choline
-
10 mM, 23% inhibition
choline
-
competitive against betaine aldehyde and uncompetitive with respect to NAD+
choline
-
mutant enzyme shows stronger inhibition compared to wild-type enzyme
cimetidine
-
-
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.
DL-glyceraldehyde
-
-
ethanolamine
-
100 mM, 35% inhibition
Glutaraldehyde
-
10 mM, 83% inhibition
glyceraldehyde
-
100 mM, 83% inhibition
glycine betaine
-
-
glycine betaine
Amaranthus sp.
-
product inhibition
glycine betaine
-
no inhibition up to 10 mM
glycine betaine
-
-
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
Hg2+
-
0.0001-0.0005 mM HgCl2
Hg2+
-
3 mM HgCl2, 90-100% inhibition
iodoacetamide
-
1 mM
iodoacetamide
-
-
iodoacetate
-
1 mM
Iodosobenzoate
-
-
Isobutanal
-
10 mM, 93% inhibition
isopentanal
-
1 mM, 84% inhibition
Isovaleraldehyde
-
wild-type enzyme shows stronger inhibition than the mutant enzyme
K+
-
1.0 mM, 35% inhibition
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
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
methyl(bis-beta-chloroethyl)amine
-
-
N,N-dimethylethanolamine
-
100 mM, 57% inhibition
N,N-Dimethylglycine
-
1 mM, 24% inhibition
n-butylaldehyde
-
10 mM, 96% inhibition
N-ethylmaleimide
-
-
N-Methylethanolamine
-
100 mM, 50% inhibition
N-methylglycine
-
1 mM, 24% inhibition
NaCl
-
inhibitory effect increases with concentrations from 50 mM to 250 mM
NaCl
-
0.5 M, 50% inhibition
NaCl
-
40% inhibition above 0.3 M
NaCl
-
mutant enzyme is slightly more sensitive to inhibition than wild-type enzyme
NaCl
Q6BD86, Q6BD88, Q6BD90, Q6BD91, Q6BD93, Q6BD95, Q6BD99, Q6BDA3, Q6BDA4, -
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
NaCl
Q155V4, -
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 30C 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
Q94IC0, Q94IC1
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
O24174, Q06DE4
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
Q8LGQ9, -
at a concentration of 0.5 M, expression of BADH2 is inhibited
NaCl
Q53CF4, -
at a concentration of 0.5 M, expression of BADH1 is inhibited; at a concentration of 0.5 M, expression of BADH2 is inhibited
NAD(P)H
-
reversible inactivation
NAD+
Amaranthus sp.
-
glycerol favours substrate inhibition
NAD+
-
substrate inhibition by high concentrations of NAD+
NADH
-
mixed inhibited against NAD+ and betaine aldehyde
NADH
-
mixed inhibitor against NAD+ and betaine aldehyde
NADH
-
product inhibition
NADP+
-
substrate inhibition above 10 mM
NADPH
-
product inhibition
NH4+
-
above 0.4 M, more than 60% inhibition
PCMB
-
0.0001-0.0005 mM
Phenylacetaldehyde
-
1 mM, 54% inhibition
Phenylarsine oxide
-
PAO
S-methyl-N,N-diethyldithiocarbamoyl sulfone
-
most potent irreversible inhibiton in vitro at 0.05 mM, but no inhibition in situ
-
S-methyl-N,N-diethyldithiocarbamoyl sulfoxide
-
irreversible inhibition
-
S-methyl-N,N-diethylthiocarbamoyl sulfone
-
irreversible inhibition
-
S-methyl-N,N-diethylthiocarbamoyl sulfoxide
-
-
-
S-methylmethanesulfonate
-
the effect of the thiol reagent MMTS on the native enzyme structure of the wild type enzyme and the mutants is examined
sodium meta-arsenite plus 2,3-dimercaptopropanol
-
arsenite-BAL
-
tetraethylamine iodide
-
10 mM, 19% inhibition
tetramethylamine iodide
-
10 mM, 19% inhibition
tetramethylammonium hydroxide
-
100 mM, 57% inhibition
tetrapropylamine iodide
-
10 mM, 43% inhibition
trimethylacetaldehyde
-
100 mM, 89% inhibition
ZnCl2
-
0.0001-0.0005 mM
ZnCl2
-
3 mM, 90-100% inhibition
Mg2+
-
0.4 M, complete inhibition
additional information
-
no substrate inhibition with NAD+
-
additional information
Amaranthus sp.
-
no product inhibition
-
additional information
-
diethyldithiocarbamic acid does not inactivate the enzyme in vitro and in situ
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Cys
-
activates, optimal concentration: 1 mM
dithiothreitol
-
enhances activity
glycine betaine
-
activates the wild-type enzyme but not the mutant enzyme
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
-
with an increase in environmental NaCl concentration, the level of BADH transcription and expression rises by activation of the promotor region
NaCl
O24174, Q06DE4
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
Q8LGQ9, -
at a concentration of 0.1 M, expression of BADH2 is increased
NaCl
Q53CF4, -
at a concentration of 0.1 M, expression of BADH1 is increased; at a concentration of 0.1 M, expression of BADH2 is increased
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
NH4+
-
slight activation up to about 0.3 M
Pro
-
0.1 M, 35% activation, at high substrate concentrations
propan-2-yl 1-thio-beta-D-galactopyranoside
-
for the expressed protein, final concentration of 1 mmol in culture solution
methanol
Q155V4, -
used in the assay as activating compound in concentration of 0.5% for 96 h
additional information
-
salt stress, drought stress, heat stress
-
additional information
-
salt stress, drought stress
-
additional information
-
salt stress, BADH1
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00000054
-
3-aminopropionaldehyde
-
pH 8.7, 37C
0.0012
-
3-aminopropionaldehyde
-
isozyme BADH2, pH and temperature not specified in the publication
0.004
-
3-aminopropionaldehyde
Q6BD86, Q6BD88, Q6BD90, Q6BD91, Q6BD93, Q6BD95, Q6BD99, Q6BDA3, Q6BDA4, -
-
0.017
-
3-aminopropionaldehyde
-
isozyme BADH1, pH and temperature not specified in the publication
3.7
-
3-aminopropionaldehyde
-, Q9S795, Q9STS1
in 100 mM sodium diphosphate pH 8.0, at 22C
0.0027
-
3-dimethylsulfoniopropionaldehyde
-
-
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
0.0037
-
4-aminobutylaldehyde
-
isozyme BADH2, pH and temperature not specified in the publication
-
0.0045
-
4-aminobutylaldehyde
-
isozyme BADH1, pH and temperature not specified in the publication
-
0.003
-
4-Aminobutyraldehyde
-
wild-type enzyme
0.004
-
4-Aminobutyraldehyde
-
mitochondrial enzyme
0.005
-
4-Aminobutyraldehyde
-
-
0.0098
-
4-Aminobutyraldehyde
-
mutant enzyme E103Q
0.024
-
4-Aminobutyraldehyde
-
cytoplasmic enzyme
0.037
-
4-Aminobutyraldehyde
-
-
0.049
-
4-Aminobutyraldehyde
Q6BD86, Q6BD88, Q6BD90, Q6BD91, Q6BD93, Q6BD95, Q6BD99, Q6BDA3, Q6BDA4, -
-
1.1
-
4-Aminobutyraldehyde
-, Q9S795, Q9STS1
in 100 mM sodium diphosphate pH 8.0, at 22C
0.000024
-
4-Guanidinobutyraldehyde
-
pH 8.7, 37C
0.00005
-
4-Guanidinobutyraldehyde
-
pH 8.7, 37C
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
0.0014
-
4-trimethylaminobutyraldehyde
-
cytoplasmic enzyme
0.014
-
acetaldehyde
-
mitochondrial enzyme
0.014
-
acetaldehyde
-
-
0.05
-
acetaldehyde
-
-
0.115
-
acetaldehyde
-
cytoplasmic enzyme
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
3.6
-
acetaldehyde
-
pH 7.7, coenzyme NAD+
28
-
acetaldehyde
-
pH 7.7, coenzyme NADP+
0.1
-
benzaldehyde
-
pH 7.7, coenzyme NAD+
6.7
-
benzaldehyde
-
pH 7.7, coenzyme NADP+
0.0000041
-
beta-NAD+
-
-
0.000005
-
Betaine aldehyde
-
pH 8.7, 37C
0.0561
-
Betaine aldehyde
-
-
0.065
-
Betaine aldehyde
-
mutant enzyme E103Q
0.068
-
Betaine aldehyde
-
wild-type enzyme
0.07716
-
Betaine aldehyde
-
-
0.0937
-
Betaine aldehyde
-
-
0.11
-
Betaine aldehyde
-
-
0.118
-
Betaine aldehyde
-
mitochondrial enzyme
0.123
-
Betaine aldehyde
-
cytoplasmic enzyme
0.127
-
Betaine aldehyde
-
-
0.133
-
Betaine aldehyde
-
-
0.1455
-
Betaine aldehyde
-
-
0.15
-
Betaine aldehyde
-
pH 7.5, 20C, native betaine-aldehyde dehydrogenase or betaine aldehyde dehydrogenase/choline dehydrogenase fusion protein
0.16
-
Betaine aldehyde
-
-
0.208
-
Betaine aldehyde
-
-
0.23
-
Betaine aldehyde
-
isozyme BADH2, pH and temperature not specified in the publication
0.26
-
Betaine aldehyde
-
-
0.291
-
Betaine aldehyde
Q6BD86, Q6BD88, Q6BD90, Q6BD91, Q6BD93, Q6BD95, Q6BD99, Q6BDA3, Q6BDA4, -
-
0.31
-
Betaine aldehyde
-
-
0.38
-
Betaine aldehyde
-
-
0.434
-
Betaine aldehyde
-
30C, pH 8.0, cosubstrate NADP+
0.506
-
Betaine aldehyde
-
30C, pH 8.0, cosubstrate NAD+
1.8
-
Betaine aldehyde
-
pH 7.7, coenzyme NADP+
2.6
-
Betaine aldehyde
-
isozyme BADH1, pH and temperature not specified in the publication
6.5
-
Betaine aldehyde
-
pH 7.7, coenzyme NAD+
6.81
-
Betaine aldehyde
-, Q9S795, Q9STS1
in 100 mM sodium diphosphate pH 8.0, at 22C
0.5
-
Butyraldehyde
-
pH 7.7, coenzyme NAD+
3.4
-
Butyraldehyde
-
pH 7.7, coenzyme NADP+
11
-
D,L-glyceraldehyde
-
pH 7.7, coenzyme NADP+
48
-
D,L-glyceraldehyde
-
pH 7.7, coenzyme NAD+
3.8
-
formaldehyde
-
pH 7.7, coenzyme NAD+
0.13
-
glycine betaine aldehyde
-
-
0.152
-
glycolaldehyde
-
mitochondrial enzyme
0.153
-
glycolaldehyde
-
-
0.24
-
glycolaldehyde
-
-
4.3
-
glycolaldehyde
-
pH 7.7, coenzyme NAD+
11.5
-
glycolaldehyde
-
pH 7.7, coenzyme NADP+
0.2
-
Isovaleraldehyde
-
pH 7.7, coenzyme NAD+
15
-
Isovaleraldehyde
-
pH 7.7, coenzyme NADP+
2.5
-
Methylglyoxal
-
pH 7.7, coenzyme NAD+
0.0025
-
NAD+
-
pH 7.7, reaction with benzaldehyde
0.004
-
NAD+
-
pH 7.7, reaction with isovaleraldehyde
0.009
-
NAD+
-
pH 7.7, reaction with undecanal
0.00946
-
NAD+
-
-
0.011
-
NAD+
-
reaction with betaine aldehyde
0.012
-
NAD+
-
pH 7.7, reaction with valeraldehyde
0.0133
-
NAD+
-
reaction with 3-dimethylsulfoniopropionaldehyde
0.019
-
NAD+
-
wild-type enzyme, reaction with betaine aldehyde
0.023
-
NAD+
-
mutant enzyme E103Q, reaction with betaine aldehyde
0.024
-
NAD+
-
mutant enzyme E103Q, reaction with 4-aminobutyraldehyde
0.026
-
NAD+
-
wild-type enzyme, reaction with 4-aminopropionaldehyde
0.028
-
NAD+
-
cytoplasmic enzyme
0.034
-
NAD+
-
mitochondrial enzyme
0.035
-
NAD+
-
-
0.04
-
NAD+
-
-
0.0445
-
NAD+
-
-
0.05
-
NAD+
-
pH 7.7, reaction with phenyl acetaldehyde
0.06
-
NAD+
-
-
0.07799
-
NAD+
-
-
0.083
-
NAD+
-
30C, pH 8.0
0.099
-
NAD+
-
-
0.136
-
NAD+
-
reaction with 4-aminobutyraldehyde
0.8
-
NAD+
-
pH 7.7, reaction with p-nitrobenzaldehyde
0.08
-
NADP+
-
pH 7.7, reaction with undecanal
0.267
-
NADP+
-
-
0.27
-
NADP+
-
pH 7.7, reaction with valeraldehyde
0.31
-
NADP+
-
pH 7.7, reaction with isovaleraldehyde
0.385
-
NADP+
-
30C, pH 8.0
0.4
-
NADP+
-
-
0.5
-
NADP+
-
-
0.61
-
NADP+
-
pH 7.7, reaction with phenyl acetaldehyde
0.635
-
NADP+
-
-
1
-
NADP+
-
pH 7.7, reaction with p-nitrobenzaldehyde
1.4
-
NADP+
-
pH 7.7, reaction with benzaldehyde
0.5
-
p-nitrobenzaldehyde
-
pH 7.7, coenzyme NAD+
51
-
phenyl acetaldehyde
-
pH 7.7, coenzyme NADP+
140
-
phenyl acetaldehyde
-
pH 7.7, coenzyme NAD+
0.8
-
propionaldehyde
-
pH 7.7, coenzyme NAD+
21
-
propionaldehyde
-
pH 7.7, coenzyme NADP+
2
3
Undecanal
-
pH 7.7, coenzyme NADP+
106
-
Undecanal
-
pH 7.7, coenzyme NAD+
0.2
-
Valeraldehyde
-
pH 7.7, coenzyme NAD+
4.1
-
Valeraldehyde
-
pH 7.7, coenzyme NADP+
9
-
Methylglyoxal
-
pH 7.7, coenzyme NADP+
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
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
261
-
NAD+
-
30C, pH 8.0
276
-
NADP+
-
30C, pH 8.0
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5.7
-
acetaldehyde
-
-
0.8705
-
AMP
-
versus NAD+
0.896
-
AMP
-
with respect to NAD+
0.7
-
benzaladehyde
-
-
0.209
-
betaine
-
30C, pH 8.0, cosubstrate NADP+
0.289
-
betaine
-
30C, pH 8.0, cosubstrate NAD+
4.6
-
Betaine aldehyde
-
-
14
-
Butyrylcholine
-
-
0.0111
-
choline
-
versus betaine aldehyde
4.1
-
choline
-
with respect to betaine aldehyde
11
-
choline
-
-
0.001
-
cimetidine
-
-
0.033
-
cimetidine
-
-
78
-
ethanolamine
-
-
7.4
-
glyceraldehyde
-
-
0.1
-
isopentanal
-
-
27
-
N,N-dimethylethanolamine
-
-
130
-
N,N-Dimethylglycine
-
-
40
-
N-Methylethanolamine
-
-
130
-
N-methylglycine
-
-
0.047
-
NADH
-
30C, pH 8.0
0.185
-
NADPH
-
30C, pH 8.0
0.53
-
Phenylacetaldehyde
-
-
26
-
tetramethylammonium hydroxide
-
-
4.5
-
trimethylacetaldehyde
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00014
-
-
NaCl level 0%, wild type
0.00015
-
-
NaCl level 1.5%, wild type
0.00017
-
-
NaCl level 1.0%, wild type
0.00045
-
-
NaCl level 0%, transgenic plant T3-5
0.00078
-
-
NaCl level 0%, transgenic plant T3-8
0.00086
-
-
NaCl level 0%, transgenic plant T3-3
0.00111
-
-
NaCl level 0%, transgenic plant T3-1
0.00119
-
-
NaCl level 0%, transgenic plant T3-9
0.0012
-
-
-
0.00523
-
-
NaCl level 1.5%, transgenic plant T3-1
0.00578
-
-
NaCl level 1.5%, transgenic plant T3-9
0.006
-
-
culture conditions, 11.1 mM glucose and 15 mM NH4Cl
0.00625
-
-
NaCl level 1.5%, transgenic plant T3-8
0.00635
-
-
NaCl level 1.0%, transgenic plant T3-1
0.00662
-
-
NaCl level 1.5%, transgenic plant T3-3
0.00723
-
-
NaCl level 1.0%, transgenic plant T3-5
0.00736
-
-
NaCl level 1.0%, transgenic plant T3-9
0.00784
-
-
NaCl level 1.0%, transgenic plant T3-3
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 30C 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.
0.00826
-
-
NaCl level 1.0%, transgenic plant T3-8
0.00881
-
-
NaCl level 1.5%, transgenic plant T3-5
0.012
-
-
culture conditions, 11.1 mM glucose, 15 mM NH4Cl and 0.4 M NaCl
0.075
-
-
BADH I
0.1938
-
-
-
0.211
-
-
culture conditions, 11.1 mM glucose, 20 mM choline and 0.4 M NaCl
0.215
-
-
culture conditions, 11.1 mM glucose and 20 mM choline
0.311
-
-
BADH II
0.492
-
-
culture conditions, 20 mM choline and 0.4 M NaCl
0.571
-
-
culture conditions, 20 mM choline
19.63
-
Q155V4, -
cloned in strain A764 and extracted, incubating at 30C 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 25C, 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
75
-
-
mutant C439V
102
-
-
mutant C439S
138
-
-
mutant C353A
165
-
-
mutant C377A
189
-
-
mutant C439A
196
-
-
wild-type enzyme
additional information
-
-
assay method
additional information
-
-
-
additional information
-
B3VMC0, B3VMC1, B3VMC2
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
-
B2BBY6
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 37C 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
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
9.5
-
-
8
-
-
reaction with 4-aminobutyraldehyde
8
-
-
Tris-HCl buffer
8
-
-
activity assay
8
-
Q6BD86, Q6BD88, Q6BD90, Q6BD91, Q6BD93, Q6BD95, Q6BD99, Q6BDA3, Q6BDA4, -
activity assay; activity assay; activity assay; activity assay; activity assay; activity assay; activity assay; activity assay; activity assay
8
-
B2BBY6
assay at
8.5
9
-
BADH I and BADH II
8.6
-
-
-
9.5
-
-
-
9.5
-
-
reaction with betaine aldehyde and propionaldehyde
9.5
-
Q6BD86, Q6BD88, Q6BD90, Q6BD91, Q6BD93, Q6BD95, Q6BD99, Q6BDA3, Q6BDA4, -
measurement of enzyme activity in dependence on pH, activity is strongly affected by the used buffer at the same pH; measurement of enzyme activity in dependence on pH, activity is strongly affected by the used buffer at the same pH; measurement of enzyme activity in dependence on pH, activity is strongly affected by the used buffer at the same pH; measurement of enzyme activity in dependence on pH, activity is strongly affected by the used buffer at the same pH; measurement of enzyme activity in dependence on pH, activity is strongly affected by the used buffer at the same pH; measurement of enzyme activity in dependence on pH, activity is strongly affected by the used buffer at the same pH; measurement of enzyme activity in dependence on pH, activity is strongly affected by the used buffer at the same pH; measurement of enzyme activity in dependence on pH, activity is strongly affected by the used buffer at the same pH; measurement of enzyme activity in dependence on pH, activity is strongly affected by the used buffer at the same pH
9.6
-
-
assay at
additional information
-
-
mutant enzyme E103Q exhibits a broader temperature optimum than the wild-type enzyme
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
8
-
pH 7.0: about 35% of maximal activity, pH 8.0: about 70% of maximal activity
7
9
-
pH 7.0: about 40% of maximal activity, pH 9.0: about 50% of maximal activity
7
9.5
-
pH 7.0: about 25% of maximal activity, pH 9.5: about 50% of maximal activity
7
9.5
-
pH 7.0: about 50% of maximal activity, pH 9.5: about 75% of maximal activity
7.8
10.1
-
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
Q6BD86, Q6BD88, Q6BD90, Q6BD91, Q6BD93, Q6BD95, Q6BD99, Q6BDA3, Q6BDA4, -
activity assay; activity assay; activity assay; activity assay; activity assay; activity assay; activity assay; activity assay; activity assay
30
-
-
activity assay
37
-
-
assay at
40
-
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
40
-
20C: about 45% of maximal activity, 40C: about 70% of maximal activity
30
-
-
assay at
additional information
-
Q155V4, -
results indicate that the tolerance of the recombinant yeasts to high temperature stress is improved remarkably as a result of improving glycine betaine content in the yeasts expressing betaine synthesis genes from Suaeda salsa
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.3
-
B2BBY6
calculated from amino acid sequence
6
-
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
activity increases between birth and 40 days of age
Manually annotated by BRENDA team
O24174, Q06DE4
source for isolating the total RNA; source for isolating the totl RNA
Manually annotated by BRENDA team
B2BBY6
found in all plant tissues excepting roots, expression level is highest in leaves and stems
Manually annotated by BRENDA team
-
higher activity in cortex than in medulla. In inner medulla, the enzyme is mainly localized in cells surrounding the tubules
Manually annotated by BRENDA team
-
localized in cortex and medulla cells
Manually annotated by BRENDA team
Q155V4, -
used for isolating RNA
Manually annotated by BRENDA team
-
leaves are used for analyzing activities of enzymes from photosystem II
Manually annotated by BRENDA team
O24174, Q06DE4
mature leaf is used for isolating total RNA; mature leaf used for isolating the total RNA
Manually annotated by BRENDA team
B2BBY6
found in all plant tissues excepting roots, expression level is highest in leaves and stems
Manually annotated by BRENDA team
O24174, Q06DE4
;
Manually annotated by BRENDA team
B3VMC0, B3VMC1, B3VMC2
found in all plant tissues excepting roots; found in all plant tissues excepting roots; found in all plant tissues excepting roots, and the transcript is detected at higher abundance in young, healthy leaves than in other tissues
Manually annotated by BRENDA team
Q155V4, -
used for isolating RNA
Manually annotated by BRENDA team
B2BBY6
find in all plant tissues excepting roots, expression level is highest in leaves and stems
Manually annotated by BRENDA team
B2BBY6
found in all plant tissues excepting roots, expression level is highest in leaves and stems
Manually annotated by BRENDA team
Q9S795, Q9STS1
source for isolating RNA; source for isolating RNA
Manually annotated by BRENDA team
Q94IC0, Q94IC1
source for isolating RNA; source for isolating RNA
Manually annotated by BRENDA team
O24174, Q06DE4
source for isolating the total RNA; source for isolating the total RNA
Manually annotated by BRENDA team
-
source for isolating RNA
Manually annotated by BRENDA team
P17202
source for isolating RNA
Manually annotated by BRENDA team
Q8LGQ9, -
source for isolating RNA; source for isolating RNA
Manually annotated by BRENDA team
Q53CF4, -
source for isolating RNA
Manually annotated by BRENDA team
B2BBY6
found in all plant tissues excepting roots, expression level is highest in leaves and stems
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
cytoplasmic and mitochondrial enzymes are products of the same gene
Manually annotated by BRENDA team
-
NAD+-linked aldehyde dehydrogenase E3 isoenzyme
Manually annotated by BRENDA team
B3VMC0, B3VMC1, B3VMC2
-
Manually annotated by BRENDA team
-
a minor isoenzyme
Manually annotated by BRENDA team
-
95% of the activity, 5% of the activity is localized in mitochondria
Manually annotated by BRENDA team
-
the enzyme is approximately equally distributed between the inner membrane and the intermembrane plus matrix fraction
Manually annotated by BRENDA team
-
5% of the activity in mitochondrial matrix, 95% of the activity in cytosol
Manually annotated by BRENDA team
-
matrix. Cytoplasmic and mitochondrial enzymes are products of the same gene
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Agrobacterium tumefaciens (strain C58 / ATCC 33970)
Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Staphylococcus aureus (strain COL)
Staphylococcus aureus (strain COL)
Staphylococcus aureus (strain COL)
Staphylococcus aureus (strain COL)
Staphylococcus aureus (strain COL)
Staphylococcus aureus (strain COL)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
53330
-
-
monomer, amino acid sequence
54600
-
O24174, Q06DE4
-
54700
-
O24174, Q06DE4
-
55000
-
B3VMC0, B3VMC1, B3VMC2
determined by gel electrophoresis
55000
-
-
about 55000 Da, isozymes BADH1 and BADH2, SDS-PAGE
55500
-
Q6BD86, Q6BD88, Q6BD90, Q6BD91, Q6BD93, Q6BD95, Q6BD99, Q6BDA3, Q6BDA4, -
estimated by SDS-PAGE; estimated by SDS-PAGE; estimated by SDS-PAGE; estimated by SDS-PAGE; estimated by SDS-PAGE; estimated by SDS-PAGE; estimated by SDS-PAGE; estimated by SDS-PAGE; estimated by SDS-PAGE
56780
-
-
mass of expressed protein (LcBADH) determinating by SDS-PAGE
61000
-
-
SDS-PAGE, Coomassie blue staining and Western blot
80000
-
B2BBY6
Expressed protein analyzed by SDSPAGE
98000
-
-
gel filtration
104000
-
-
BADH I and BADH II, disc gradient gel electrophoresis
110000
-
-
gel filtration
115000
120000
-
gel filtration
120000
-
-
gel filtration
125000
-
Amaranthus sp.
-
-
139000
-
-
gel filtration
145000
-
-
gel filtration
220000
-
-
gel filtration
230000
-
-
-
230000
-
-
for the homotetramer
232000
-
-
gel filtration
250000
-
-
betaine aldehyde dehydrogenase/choline dehydrogenase fusion protein, gel filtration
494000
-
-
cytoplasmic enzyme
688000
-
-
non-denaturing PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 54267, calculation from nucleotide sequence
?
-
x * 52000, SDS-PAGE
?
-
x * 54000, SDS-PAGE
?
-
x * 53000 + x * 59000, SDS-PAGE
?
-
2 * 117000, betaine aldehyde dehydrogenase/choline dehydrogenase fusion protein, SDS-PAGE
dimer
-
2 * 63000, SDS-PAGE
dimer
-
1 * 40000 + 1 * 64000, BADH II, SDS-PAGE
dimer
-
2 * 60000, SDS-PAGE
dimer
Amaranthus sp.
-
1 * 63000 + 1 * 70000, SDS-PAGE
dimer
-
2 * 61000, SDS-PAGE
dimer
-
2 * 61000, SDS-PAGE
dimer
O24174, Q06DE4
;
homotetramer
-
-
homotetramer
-
x-ray crystallography
oligomer
B3VMC0, B3VMC1, B3VMC2
-
tetramer
-
4 * 55000, SDS-PAGE
tetramer
-
4 * 58000, SDS-PAGE
tetramer
-
4 * 55000, cytoplasmic enzyme, SDS-PAGE
tetramer
-
at pH 7.0 in the absence of K+ in a buffer of low ionic strength, the active tetrameric form dissociates into inactive monomers
tetramer
-
at pH 7.0 in the absence of K+ in a buffer of low ionic strength, the active tetrameric form dissociates into inactive dimers
tetramer
-
4 x 61000, SDS-PAGE
tetramer
Cylindrocarpon didymum M-1
-
4 * 58000, SDS-PAGE
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
side-chain modification Attention: controlled vocabulary for this datafield
B3VMC0, B3VMC1, B3VMC2
commentary
proteolytic modification
-
enzyme may be processed in the mitochondria
proteolytic modification
-
transit peptide may comprise only 7 or 8 residues
proteolytic modification
-
enzyme is synthesisized as a precursor of 1200 Da higher than the mature enzyme
additional information
Amaranthus sp.
-
no glycosylation
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging-drop method
-
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
-
BADH in the presence of 2-mercaptoethanol, glycerol, NADP+ and 150 mM K+, hanging drop vapor diffusion method, using 85 mM HEPESNaOH, pH 7.5, 8.5% (v/v) isopropanol, 17% (w/v) polyethylene glycol 4000 and 15% (v/v) glycerol, at 18C; the three dimensional structure of betaine aldehyde dehydrogenase, in complex with glycerol, NADP+ and K+ ions, is determined at 2.1 A resolution
-
native and mutant enzyme C286A in complex with NADPH, hanging drop vapor diffusion method, using 85 mM HEPES/NaOH buffer, pH 7.5, 8.5% (v/v) propan-2-ol, 17% (w/v) PEG 4000, and 15% (v/v) glycerol
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
-
-
15 h, 80% loss of activity
5
11
-
mutant enzyme is less stable than the wild-type enzyme in the pH-range 5-11
5
7.5
-
15 h, stable
5.5
9.5
-
stable
6.5
-
-
most stable at
8
-
-
15 h, 60% loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
34.3
-
-
apparent T50 mutant C439V
37
-
-
apparent T50 mutant C439S
40
-
-
pH 7.4, 0.01% 2-mercaptoethanol, 7 min, 50% loss of activity
40
-
-
loss of activity, activity is regained, when the heated enzyme is cooled to 30C or lower
43.6
-
-
apparent T50 mutant C439A
45
-
-
120 min, about 80% decrease of activity
46
-
-
apparent T50 mutant C377A
49.4
-
-
apparent T50 mutant C353A
50
-
-
pH 7.4, 0.01% 2-mercaptoethanol, 7 min, complete loss of activity
50
-
-
120 min, about 75% loss of activity
50
-
-
120 min, complete inactivation
50.7
-
-
apparent T50 wild-type enzyme
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
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the enzyme is stable in absence of K+ even at very low enzyme concentrations
-
addition of glycerol and 2-mercaptoethanol effectively stabilizes the enzyme
-
complete loss of activity when dialyzed against 10 mM buffer, pH 8.0, addition of 20% glycerol stabilizes
-
salt-tolerant enzyme retains 50% of its initial activity at 1.2 M K+
-
total RNA of leaves subjected to RT-PCR analysis to examine the influence of environmental stress like drought, salt or heat on BADH expression. Results showed tha JcBD1 gene transcripts of those plants exposed to 30% PEG, 300 mM NaCl or 50C heat stress were obviously higher than that of the control plants. JcBD1 mRNA levels in stress treated leaved are increased by 79% or more, as compared with the control, which strongly confirms that mRNA expression are relative to abiotic stress.
B2BBY6
at the optimum pH of 8.0 the enzyme is inactivated by dilution, it is stable at pH 6.5 even at very low concentrations
-
dialysis for 5 days against 0.1 M buffer, pH 7.4, at 4C, stable
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
conformational change induced by coenzyme or the aldehyde might be important for both proper enzyme function and protection against oxidation
-
655203
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80C, frozen in presence of 10 mM dithiothreitol, stable for several months without appreciable loss of activity
-
-20C, 9.1 M buffer, pH 7.4, 3 weeks, stable
-
-20C, 10% loss of activity after 3 months
-
-70C, with repeated freezing and thawing, stable for at least 1 month
-
-80C, less than 30% loss of activity after 18 months
-
-70C, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-
Amaranthus sp.
-
His-Tag affinity chromatography; His-Tag affinity chromatography
-, Q9S795, Q9STS1
recombinant enzyme
-
aldehyde dehydrogenase E3 isozyme is a betaine aldehyde dehydrogenase
-
For purification of the recombinant protein, cells of 500 ml culture are harvested. Pellet is suspended in lysis buffer and suspension was incubated. Following sonication, suspension is centrifuged. Clear supernatant is collected and loaded onto a Glutathione-Agarose column equilibrated with buffer (20 mM Tris-HCl (pH 8.0), 5.0 mM EDTA). The recombinant protein is eluted with elution buffer (20 mM Tris-HCl (pH 8.0), 5.0 mM EDTA, and 1.0 mM reduced glutathione). Eluted protein is collected and the purity is analyzed by 12% SDS-PAGE. To remove the GST moiety, the recombinant proteins are digested with PreScission protease.
B2BBY6
Ni Sepharose affinity column chromatography, and gel filtration
-
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
B3VMC0, B3VMC1, B3VMC2
; by a two step procedure
-
purified on Q-Sepharose fast flow and 2', 5'-ADP-Sepharose columns, 28 mg of pure protein per liter of culture are yielded
-
purified to homogeneity following a two-step procedure
-
purified to homogeneity following a two-step procedure, proteins expressed in Escherichia coli
-
rapid purification
-
2 enzyme forms: BADH I and BADH II
-
the protein undergoes several chromatographic and dialysis steps during purification
-
on GSTrap FF columns; on GSTrap FF columns; on GSTrap FF columns; on GSTrap FF columns; on GSTrap FF columns; on GSTrap FF columns; on GSTrap FF columns; on GSTrap FF columns; on GSTrap FF columns
Q6BD86, Q6BD88, Q6BD90, Q6BD91, Q6BD93, Q6BD95, Q6BD99, Q6BDA3, Q6BDA4, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
-, Q9S795, Q9STS1
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 Arabidopsis are of expected size for correctly processed transcripts. Sequencing analysis of 4 cDNA clones confirms the correct processing.; 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 Arabidopsis are of expected size for correctly processed transcripts. Sequencing analysis of 4 cDNA clones confirms the correct processing.
Q9S795, Q9STS1
expressed in trifoliate orange Poncirus trifoliata by Agrobacterium-mediated transformation
-
Seeds from T2 generation (lines T2-1, T2-3, T2-5, T2-8 and T2-9) of transgenic tomato containing the BADH gene from Atriplex hortensis were used
-
expression in Escherichia coli
-
high-level expression of betaine aldehyde dehydrogenase in cultured cells, roots, and leaves of carrot via plastid genetic engineering. Homoplasmic transgenic plants that exhibit high levels of salt tolerance are regenerated from bombarded cell cultures via somatic embryogenesis. Transformation efficiency of carrot somatic embryos is very high, with one transgenic event per approximately seven bombarded plates under optimal conditions. In vitro transgenic carrot cells transformed with the badh transgene are visually green in color when compared to untransformed carrot cells, this offers a visual selection for transgenic lines. Transgenic carrot plants expressing BADH grow in presence of high concentrations of NaCl, up to 400 mM
-
construction of a betaine aldehyde dehydrogenase/choline dehydrogenase fusion protein and expression in Escherichia coli and Nicotiana tabacum. Escherichia coli cells expressing the fusion protein are able to grow to higher final densities and to accumulate more glycine betaine than cells expressing choline dehydrogenase alone
-
expression in Escherichia coli and Salmonella typhimurium
-
To determine whether the unusual events occurring in the transcripts are specific only to the rice genome, RT-PCR experiments using the total RNA extracted from seedlings of barley are performed. These experiments use primers either to amplify the full length of mRNA or exclusively the 5' region of BADH homologs corresponding to those in rice. The sequencing data from a total of 5 cDNA clones demonstrate that all the tested cDNA clones have deletions of the 5' exonic sequences resulting from the unusual posttranscriptional processing.; To determine whether the unusual events occurring in the transcripts were specific only to the rice genome, RT-PCR experiments using the total RNA extracted from seedlings of barley are performed. These experiments use primers either to amplify the full length of mRNA or exclusively the 5' region of BADH homologs corresponding to those in rice. The sequencing data from a total of 6 cDNA clones demonstrate that all the tested cDNA clones have deletions of the 5' exonic sequences resulting from the unusual posttranscriptional processing.
Q94IC0, Q94IC1
expressed in Escherichia coli BL21
B2BBY6
the BADH gene of Leymus chinensis is cloned by RT-PCR and RACE technology and is designated as LcBADH. The cDNA sequence of LcBADH is 1774 bp including the open reading frame of 1521 bp (coding 506 amino acids). The vector of prokaryotic expression is constructed by inserting the LcBADH gene fragment into pET30a(+) and transformed into Escherichia coli BL21(DE3)
-
expressed in Nicotiana tabacum
Q153G6
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli strain BL21
-
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.; 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.
O24174, Q06DE4
in Escherichia coli strain BL21 (DE3); in Escherichia coli strain BL21 (DE3); in Escherichia coli strain BL21 (DE3)
B3VMC0, B3VMC1, B3VMC2
into the pGEM-T easy vector for sequencing; into the pGEM-T easy vector for sequencing
O24174, Q06DE4
expressed in Escherichia coli
-
expressed in Escherichia coli; plasmid pCALbetB containing the full sequence of the gene betB that encodes PaBADH is used for the expression of the enzyme in Escherichia coli cells
-
expression in Escherichia coli cells
-
the gene betB, encoding for Pseudomonas aeruginosa betaine-aldehyde dehydrogenase, is cloned into a pCAL-n vector for sequencing and protein expression in Escherichia coli
-
wild type Pseudomonas aeruginosa betaine aldehyde dehydrogenase and the four mutants C353A, C377A, C439A and C286A
-
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 tomato are of expected size for correctly processed transcripts. Sequencing analysis of 3 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
-
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.
P17202
expression in Nicotiana tabacum 89. Tobacco expressing BADH survives on Murashige-Skoog medium containing 200 mM NaCl, whereas the untransformed plants turn yellow after 20 d and die
Q8W5A1, -
partial characterization of the full-length BADH promoter of Suaeda liaotungensis through fusions of various lengths fused to the beta-glucuronidase coding sequence and subsequent expression in tobacco leaves treatment with NaCl are reported
-
cloned in different strains (A764, A765, A767 and YPIC3) of Pichia pastoris
Q155V4, -
To determine whether the unusual events occurring in the transcripts are specific only to the rice genome, RT-PCR experiments using the total RNA extracted from seedlings of wheat are performed. These experiments use primers either to amplify the full length of mRNA or exclusively the 5' region of BADH homologs corresponding to those in rice. Sequencing data from 22 DNA clones demonstrate that all the tested cDNA clones had deletion(s) of the 5' exonic sequences resulting from the unusual posttranscriptional processing.; To determine whether the unusual events occurring in the transcripts are specific only to the rice genome, RT-PCR experiments using the total RNA extracted from seedlings wheat are performed. These experiments use primers either to amplify the full length of mRNA or exclusively the 5' region of BADH homologs corresponding to those in rice. Sequencing data from 4 DNA clones demonstrate that all the tested cDNA clones had deletion(s) of the 5' exonic sequences resulting from the unusual posttranscriptional processing.
Q8LGQ9, -
To determine whether the unusual events occurring in the BADH transcripts are specific only to the rice genome, RT-PCR experiments using the total RNA extracted from seedlings of maize species are carried out. These experiments used primers either to amplify the full length of mRNA or exclusively the 5' region of BADH homologs corresponding to those in rice. The sequencing data from a total of 6 cDNA clones demonstrate that all the tested cDNA clones have deletion(s) of the 5' exonic sequences resulting from the unusual posttranscriptional processing.; To determine whether the unusual events occurring in the transcripts are specific only to the rice genome, RT-PCR experiments using the total RNA extracted from seedlings of maize are performed. These experiments use primers either to amplify the full length of mRNA or exclusively the 5' region of BADH homologs corresponding to those in rice. The sequencing data from a total of 9 cDNA clones demonstrate that all the tested cDNA clones have deletions of the 5' exonic sequences resulting from the unusual posttranscriptional processing.
Q53CF4, -
into the pCR2.1-TOPO and pGEX-6p-2 vector for sequencing of the coding region and expression of the enzyme in Escherichia coli BL21, respectively; into the pCR2.1-TOPO and pGEX-6p-2 vector for sequencing of the coding region and expression of the enzyme in Escherichia coli BL21, respectively; into the pCR2.1-TOPO and pGEX-6p-2 vector for sequencing of the coding region and expression of the enzyme in Escherichia coli BL21, respectively; into the pCR2.1-TOPO and pGEX-6p-2 vector for sequencing of the coding region and expression of the enzyme in Escherichia coli BL21, respectively; into the pCR2.1-TOPO and pGEX-6p-2 vector for sequencing of the coding region and expression of the enzyme in Escherichia coli BL21, respectively; into the pCR2.1-TOPO and pGEX-6p-2 vector for sequencing of the coding region and expression of the enzyme in Escherichia coli BL21, respectively; into the pCR2.1-TOPO and pGEX-6p-2 vector for sequencing of the coding region and expression of the enzyme in Escherichia coli BL21, respectively; into the pCR2.1-TOPO and pGEX-6p-2 vector for sequencing of the coding region and expression of the enzyme in Escherichia coli BL21, respectively; into the pCR2.1-TOPO and pGEX-6p-2 vector for sequencing of the coding region and expression of the enzyme in Escherichia coli BL21, respectively
Q6BD86, Q6BD88, Q6BD90, Q6BD91, Q6BD93, Q6BD95, Q6BD99, Q6BDA3, Q6BDA4, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the ALDH10A8 gene is weakly induced by abscisic acid, salt, chilling (4C), methyl viologen and dehydration; the ALDH10A9 gene is weakly induced by abscisic acid, salt, chilling (4C), methyl viologen and dehydration
-, Q9S795, Q9STS1
the expression of isozymes BADH1 and BADH2 is decreased by the submerged treatment and recovered to control (0 h) level after re-aeration
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C286A
-
cysteine 286 plays an important role in the maintenance ot the tetrameric structure
C286A
-
mutant with reduced reactivity
C353A
-
cysteine 353 not essential for enzyme activity
C353A
-
steady-state kinetic and structure not significantly affected
C353A
-
mutant, shows similar inactivation kinetics to the wild-type enzyme
C377A
-
cysteine 377 not essential for enzyme activity
C377A
-
steady-state kinetic and structure not significantly affected
C377A
-
mutant, shows similar inactivation kinetics to the wild-type enzyme
C439A
-
cysteine 439 not essential for enzyme activity
C439A
-
steady-state kinetic and structure not significantly affected, stability severely reduced
C439A
-
mutant, shows similar inactivation kinetics to the wild-type enzyme
C439S
-
steady-state kinetic and structure not significantly affected, stability severely reduced
C439V
-
steady-state kinetic and structure not significantly affected, stability severely reduced
E103K
-
mutant enzyme has no activity with betaine aldehyde and 4-aminobutyraldehyde
E103Q
-
Km-values for 4-aminobutyraldehyde increases compared to wild-type
E103Q
-
mutant enzyme is slightly more sensitive to inhibition by NaCl but less sensitive to inhibition by (NH4)2SO4. Glycine betaine activates the wild-type enzyme but not the mutant enzyme. Mutant enzyme shows stronger inhibition by choline compared to wild-type enzyme. Wild-type enzyme shows stronger inhibition by isovaleraldehyde than the mutant enzyme.Mutant enzyme exhibits a broader temperature optimum than the wild-type enzyme. Mutant enzyme appears to be more heat labile than the wild-type enzyme. Mutant enzyme is less stable than the wild-type enzyme in the pH-range 5-11. Mutant enzyme 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
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-mercaptoethanol, Reactivation of DSF-inactivated enzyme with 10 mM 2-mercaptoethanol; DTT, Reactivation of disulfiram-inactivated enzyme with 5 mM DTT; GSH, Reactivation of DSF-inactivated with 10 mM GSH
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
energy production
B2BBY6
the seed of the plant is the raw material for biodiesels
agriculture
-
potential: the BADH gene can be cloned from Leymus chinensis under stress treatment, which indicates that its expression and regulation may play an important role in stress tolerance. Therefore, it can be transformed into other plants to obtain transgenic species with a high saline-alkali tolerance by biotechnology; as a result, it can speed up the recovering and rebuilding of saline-alkaline grassland
medicine
-
Pseudomonas aeruginosa is an important pathogen, glycine betaine could play an important physiological role under the conditions present in the infection sites
medicine
-
betaine aldehyde dehydrogenase is a potential target for antimicrobial agents against Pseudomonas aeruginosa
medicine
-
PaBADH could be an antimicrobial target
medicine
-
the enzyme could be a target for antibiotic design
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
agriculture
-
gene expression under the control of inducible promoters is preferred in any strategy to produce transgenic plants with transgene-mediated improvements in resistance to salt.