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Information on EC 1.2.1.8 - betaine-aldehyde dehydrogenase and Organism(s) Homo sapiens

for references in articles please use BRENDA:EC1.2.1.8
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EC Tree
IUBMB Comments
In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria. In contrast, different enzymes are involved in the first reaction. In plants, this reaction is catalysed by EC 1.14.15.7 (choline monooxygenase), whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase) . In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase).
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Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
badh2, badh1, pabadh, osbadh2, betaine-aldehyde dehydrogenase, betaine aldehyde dehydrogenase 2, osbadh1, pkbadh, badh2-e7, badh2-e2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
BADH
-
-
-
-
betaine aldehyde dehydrogenase
-
-
-
-
betaine aldehyde oxidase
-
-
-
-
dehydrogenase, betaine aldehyde
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
betaine-aldehyde:NAD+ oxidoreductase
In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria. In contrast, different enzymes are involved in the first reaction. In plants, this reaction is catalysed by EC 1.14.15.7 (choline monooxygenase), whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase) [5]. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase).
CAS REGISTRY NUMBER
COMMENTARY hide
9028-90-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH
show the reaction diagram
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH
show the reaction diagram
-
-
-
-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH
show the reaction diagram
-
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cimetidine
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005
4-Aminobutyraldehyde
-
-
0.05
acetaldehyde
-
-
0.24
glycolaldehyde
-
-
0.035
NAD+
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001
cimetidine
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
reaction with 4-aminobutyraldehyde
9.5
-
reaction with betaine aldehyde and propionaldehyde
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
NAD+-linked aldehyde dehydrogenase E3 isoenzyme
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AL7A1_HUMAN
539
0
58487
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
230000
-
-
54000
-
x * 54000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 54000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
aldehyde dehydrogenase E3 isozyme is a betaine aldehyde dehydrogenase
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chern, M.K.; Pietruszko, R.
Human aldehyde dehydrogenase E3 isozyme is a betaine aldehyde dehydrogenase
Biochem. Biophys. Res. Commun.
213
561-568
1995
Homo sapiens
Manually annotated by BRENDA team
Chern, M.K.; Pietruszko, R.
Evidence for mitochondrial localization of betaine aldehyde dehydrogenase in rat liver: purification, characterization, and comparison with human cytoplasmic E3 isozyme
Biochem. Cell Biol.
77
179-187
1999
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team