Any feedback?
Information on EC 1.2.1.8 - betaine-aldehyde dehydrogenase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9HTJ1
for references in articles please use BRENDA:EC1.2.1.8Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.2.1.8 betaine-aldehyde dehydrogenaseIUBMB Comments
In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria. In contrast, different enzymes are involved in the first reaction. In plants, this reaction is catalysed by EC 1.14.15.7 (choline monooxygenase), whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase) . In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase).
Specify your search results
Word Map
- 1.2.1.8
-
badhs
- aroma
-
fragrant
-
2-acetyl-1-pyrroline
-
osmoprotectant
- molecular biology
-
basmati
-
non-fragrant
-
scent
- 4-aminobutyraldehyde
- medicine
- 3-aminopropionaldehyde
-
non-aromatic
- aminoaldehyde
-
jasmine
- agriculture
- biotechnology
- energy production
- food industry
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
badh2, badh1, pabadh, osbadh2, betaine-aldehyde dehydrogenase, betaine aldehyde dehydrogenase 2, osbadh1, pkbadh, badh2-e7, badh2-e2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BADH
betaine aldehyde dehydrogenase
betaine aldehyde oxidase
-
-
-
-
dehydrogenase, betaine aldehyde
-
-
-
-
BADH
-
-
-
-
betaine aldehyde dehydrogenase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
steady-state ordered mechanism, in which NAD+ binds first and NADH leaves last
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
oxidation
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
betaine-aldehyde:NAD+ oxidoreductase
In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria. In contrast, different enzymes are involved in the first reaction. In plants, this reaction is catalysed by EC 1.14.15.7 (choline monooxygenase), whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase) [5]. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase).
CAS REGISTRY NUMBER
COMMENTARY
9028-90-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
betaine aldehyde + NAD(P)+ + H2O
betaine + NAD(P)H + H+
-
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + 2 H+
-
-
-
r
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
ir
betaine aldehyde + NADP+ + H2O
glycine betaine + NADPH + H+
-
-
-
ir
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
-
no activity
-
-
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + 2 H+
-
-
-
-
ir
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
-
-
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH
-
preferentially uses NADP+ over NAD+
-
-
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
-
-
-
ir
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
-
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
reverse reaction not detected
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
preferentially uses NADP+ over NAD+
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
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
-
inducible enzyme accumulates in the presence of choline, acetylcholine or betaine in the medium
-
-
?
betaine aldehyde + NADP+ + H2O
betaine + NADPH + H+
-
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
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
?
-
-
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
?
-
-
no activity with 3-dimethylsulfoniopropionaldehyde
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + 2 H+
-
-
-
r
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
-
-
-
ir
betaine aldehyde + NADP+ + H2O
glycine betaine + NADPH + H+
-
-
-
ir
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + 2 H+
-
-
-
-
ir
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
-
-
-
-
?
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
-
-
-
ir
betaine aldehyde + NAD(P)+ + H2O
glycine betaine + NAD(P)H + H+
-
-
-
ir
betaine aldehyde + NAD+ + H2O
betaine + NADH
-
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
-
inducible enzyme accumulates in the presence of choline, acetylcholine or betaine in the medium
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
K+
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+
the enzyme requires K+ ions for stability and possesses two K+ binding sites per subunit
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-methyl-N,N-diethyldithiocarbamoyl sulfone
most potent irreversible inhibition 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
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
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
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
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
S-methylmethanesulfonate
-
the effect of the thiol reagent MMTS on the native enzyme structure of the wild type enzyme and the mutants is examined
additional information
diethyldithiocarbamic acid does not inactivate the enzyme in vitro and in situ
-
additional information
-
diethyldithiocarbamic acid does not inactivate the enzyme in vitro and in situ
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.012
culture conditions, 11.1 mM glucose, 15 mM NH4Cl and 0.4 M NaCl
0.211
culture conditions, 11.1 mM glucose, 20 mM choline and 0.4 M NaCl
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9.5
7 - 9.5
-
pH 7.0: about 50% of maximal activity, pH 9.5: about 75% of maximal activity
7 - 9.5
-
pH 7.0: about 25% of maximal activity, pH 9.5: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
tetramer
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
the three dimensional structure of betaine aldehyde dehydrogenase, in complex with glycerol, NADP+ and K+ ions, is determined at 2.1 A resolution
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 18°C
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C286A
-
cysteine 286 plays an important role in the maintenance ot the tetrameric structure
C353A
C377A
C439A
C439S
-
steady-state kinetic and structure not significantly affected, stability severely reduced
C439V
-
steady-state kinetic and structure not significantly affected, stability severely reduced
C353A
-
mutant, shows similar inactivation kinetics to the wild-type enzyme
C377A
-
mutant, shows similar inactivation kinetics to the wild-type enzyme
C439A
-
steady-state kinetic and structure not significantly affected, stability severely reduced
C439A
-
mutant, shows similar inactivation kinetics to the wild-type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
50
-
pH 7.4, 0.01% 2-mercaptoethanol, 7 min, complete loss of activity
40
-
loss of activity, activity is regained, when the heated enzyme is cooled to 30°C or lower
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-
OXIDATION STABILITY
ORGANISM
UNIPROT
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
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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, proteins expressed in Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nagasawa, T.; Kawabata, Y.; Tani, Y.; Ogata, K.
Purification and characterization of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa A-16
Agric. Biol. Chem.
40
1743-1749
1976
Pseudomonas aeruginosa, Pseudomonas aeruginosa A-16
-
Figueroa-Soto, C.G.; Lopez-Cervantes, G.; Valenzuela-Soto, E.M.
Immunolocalization of betaine aldehyde dehydrogenase in porcine kidney
Biochem. Biophys. Res. Commun.
258
732-736
1999
Amaranthus hypochondriacus, Amaranthus palmeri, Pseudomonas aeruginosa, Sus scrofa
Velasco-Garcia, R.; Mujica-Jimenez, C.; Mendoza-Hernandez, G.; Munoz-Clares, R.A.
Rapid purification and properties of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa
J. Bacteriol.
181
1292-1300
1999
Pseudomonas aeruginosa
Gonzalez-Segura, L.; Velasco-Garcia, R.; Munoz-Clares, R.A.
Modulation of the reactivity of the essential cysteine residue of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa
Biochem. J.
361
577-585
2002
Pseudomonas aeruginosa
Munoz-Clares, R.A.; Gonzalez-Segura, L.; Mujica-Jimenez, C.; Contreras-Diaz, L.
Ligand-induced conformational changes of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa and Amaranthus hypochondriacus L. leaves affecting the reactivity of the catalytic thiol
Chem. Biol. Interact.
143-144
129-137
2003
Amaranthus hypochondriacus, Pseudomonas aeruginosa
Valenzuela-Soto, E.M.; Velasco-Garcia, R.; Mujica-Jimenez, C.; Gaviria-Gonzalez, L.L.; Munoz-Clares, R.A.
Monovalent cations requirements for the stability of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa, porcine kidney and amaranth leaves
Chem. Biol. Interact.
143-144
139-148
2003
Amaranthus hypochondriacus, Pseudomonas aeruginosa, Sus scrofa
Velasco-Garcia, R.; Chacon-Aguilar, V.M.; Hervert-Hernandez, D.; Munoz-Clares, R.A.
Inactivation of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa and Amaranthus hypochondriacus L. leaves by disulfiram
Chem. Biol. Interact.
143-144
149-158
2003
Amaranthus hypochondriacus, Pseudomonas aeruginosa
Velasco-Garcia, R.; Gonzalez-Segura, L.; Munoz-Clares, R.A.
Steady-state kinetic mechanism of the NADP+- and NAD+-dependent reactions catalysed by betaine aldehyde dehydrogenase from Pseudomonas aeruginosa
Biochem. J.
352
675-683
2000
Pseudomonas aeruginosa
Velasco-Garcia, R.; Villalobos, M.A.; Ramirez-Romero, M.A.; Mujica-Jimenez, C.; Iturriaga, G.; Munoz-Clares, R.A.
Betaine aldehyde dehydrogenase from Pseudomonas aeruginosa: cloning, over-expression in Escherichia coli, and regulation by choline and salt
Arch. Microbiol.
185
14-22
2006
Pseudomonas aeruginosa (Q9HTJ1)
Velasco-Garcia, R.; Zaldivar-Machorro, V.J.; Mujica-Jimenez, C.; Gonzalez-Segura, L.; Munoz-Clares, R.A.
Disulfiram irreversibly aggregates betaine aldehyde dehydrogenase--a potential target for antimicrobial agents against Pseudomonas aeruginosa
Biochem. Biophys. Res. Commun.
341
408-415
2006
Pseudomonas aeruginosa
Gonzalez-Segura, L.; Velasco-Garcia, R.; Rudino-Pinera, E.; Mujica-Jimenez, C.; Munoz-Clares, R.A.
Site-directed mutagenesis and homology modeling indicate an important role of cysteine 439 in the stability of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa
Biochimie
87
1056-1064
2005
Pseudomonas aeruginosa
Munoz-Clares, R.A.; Diaz-Sanchez, A.G.; Gonzalez-Segura, L.; Montiel, C.
Kinetic and structural features of betaine aldehyde dehydrogenases: Mechanistic and regulatory implications
Arch. Biochem. Biophys.
493
71-81
2010
Pseudomonas aeruginosa (Q9HTJ1), Pseudomonas aeruginosa
Gonzalez-Segura, L.; Mujica-Jimenez, C.; Munoz-Clares, R.A.
Reaction of the catalytic cysteine of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa with arsenite-BAL and phenylarsine oxide
Chem. Biol. Interact.
178
64-69
2009
Pseudomonas aeruginosa
Gonzalez-Segura, L.; Rudino-Pinera, E.; Munoz-Clares, R.A.; Horjales, E.
The crystal structure of a ternary complex of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa provides new insight into the reaction mechanism and shows a novel binding mode of the 2-phosphate of NADP+ and a novel cation binding site
J. Mol. Biol.
385
542-557
2009
Pseudomonas aeruginosa, Pseudomonas aeruginosa (Q9HTJ1)
Zaldivar-Machorro, V.J.; Lopez-Ortiz, M.; Demare, P.; Regla, I.; Munoz-Clares, R.A.
The disulfiram metabolites S-methyl-N,N-diethyldithiocarbamoyl sulfoxide and S-methyl-N,N-diethylthiocarbamoyl sulfone irreversibly inactivate betaine aldehyde dehydrogenase from Pseudomonas aeruginosa, both in vitro and in situ, and arrest bacterial grow
Biochimie
93
286-295
2011
Pseudomonas aeruginosa (Q9HTJ1), Pseudomonas aeruginosa
Diaz-Sanchez, A.; Gonzalez-Segura, L.; Rudino-Pinera, E.; Lira-Rocha, A.; Torres-Larios, A.; Munoz-Clares, R.
Novel NADPH-cysteine covalent adduct found in the active site of an aldehyde dehydrogenase
Biochem. J.
439
443-452
2011
Pseudomonas aeruginosa (Q9HTJ1), Pseudomonas aeruginosa
EXTERNAL LINKS (specific for EC-Number 1.2.1.8)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
