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Information on EC 1.2.1.48 - long-chain-aldehyde dehydrogenase and Organism(s) Mus musculus and UniProt Accession E9Q3E1

for references in articles please use BRENDA:EC1.2.1.48
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EC Tree
IUBMB Comments
The best substrate is dodecylaldehyde.
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This record set is specific for:
Mus musculus
UNIPROT: E9Q3E1
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
fatty aldehyde dehydrogenase, aldh3b2, aldh10, long-chain aldehyde dehydrogenase, aldh3b3, falddh, long-chain fatty aldehyde dehydrogenase, membrane-bound fatty aldehyde dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ALDH3A2
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dehydrogenase, long-chain aliphatic aldehyde
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fatty aldehyde dehydrogenase
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fatty aldehyde:NAD+ oxidoreductase
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long-chain aldehyde dehydrogenase
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long-chain fatty aldehyde dehydrogenase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
long-chain-aldehyde:NAD+ oxidoreductase
The best substrate is dodecylaldehyde.
CAS REGISTRY NUMBER
COMMENTARY hide
59298-89-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
hexadecanal + NAD+ + H2O
hexadecanoate + NADH + 2 H+
show the reaction diagram
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-
?
cis,cis-9,12-octadecadienal + NAD+ + H2O
cis,cis-9,12-octadecadienoic acid + NADH
show the reaction diagram
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major substrate
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-
?
hexadecanal + NAD+ + H2O
hexadecanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
long-chain aldehyde + NAD+ + H2O
long-chain acid anion + NADH
show the reaction diagram
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-
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?
pyrenedecanal + NAD+ + H2O
pyrenedecanoic acid + NADH
show the reaction diagram
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-
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?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cis,cis-9,12-octadecadienal + NAD+ + H2O
cis,cis-9,12-octadecadienoic acid + NADH
show the reaction diagram
-
major substrate
-
-
?
long-chain aldehyde + NAD+ + H2O
long-chain acid anion + NADH
show the reaction diagram
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-
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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low activity
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
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high activity
Manually annotated by BRENDA team
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low activity
Manually annotated by BRENDA team
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high activity
Manually annotated by BRENDA team
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high activity
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme is a member of the ALDH3 family
physiological function
ALDH3 family members (ALDH3A1, ALDH3A2, ALDH3B1, ALDH3B2 and ALDH3B3) are responsible for the removal of lipid-derived aldehydes. Isozyme ALDH3B2 probably acts to remove lipid-derived aldehydes in lipid droplets generated via oxidative stress as a quality control mechanism
evolution
the enzyme is a member of the ALDH3 family
physiological function
ALDH3 family members (ALDH3A1, ALDH3A2, ALDH3B1, ALDH3B2 and ALDH3B3) are responsible for the removal of lipid-derived aldehydes
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AL3B2_MOUSE
479
0
52983
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
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2 * 55000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 55000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoprotein
enzyme ALDH3B2 is modified by prenylation at its C-terminus. The modification greatly influences its membrane localization and enzymatic activity towards hexadecanal
lipoprotein
enzyme ALDH3B3 is modified by prenylation at its C-terminus. The modification greatly influences its membrane localization and enzymatic activity towards hexadecanal
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Keller, M.; Watschinger, K.; Golderer, G.; Maglione, M.; Sarg, B.; Lindner, H.; Werner-Felmayer, G.; Terrinoni, A.; Wanders, R.; Werner, E.
Monitoring of fatty aldehyde dehydrogenase by formation of pyrenedecanoic acid from pyrenedecanal
J. Lipid Res.
51
1554-1559
2010
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Kitamura, T.; Takagi, S.; Naganuma, T.; Kihara, A.
Mouse aldehyde dehydrogenase ALDH3B2 is localized to lipid droplets via two C-terminal tryptophan residues and lipid modification
Biochem. J.
465
79-87
2015
Mus musculus (E9Q3E1), Mus musculus (J3QMK6), Mus musculus
Manually annotated by BRENDA team