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1.2.1.48: long-chain-aldehyde dehydrogenase

This is an abbreviated version!
For detailed information about long-chain-aldehyde dehydrogenase, go to the full flat file.

Word Map on EC 1.2.1.48

Reaction

a long-chain aldehyde
+
NAD+
 +
H2O
=
a long-chain carboxylate
 +
NADH
 +
H+

Synonyms

ALDH, ALDH10, ALDH3A2, Aldh3b1, ALDH3B2, ALDH3B3, Bt-Aldh, dehydrogenase, long-chain aliphatic aldehyde, FAldDH, FALDH, fatty aldehyde dehydrogenase, fatty aldehyde:NAD+ oxidoreductase, long-chain aldehyde dehydrogenase, long-chain fatty aldehyde dehydrogenase, long-chain-aldehyde dehydrogenase, membrane-bound fatty aldehyde dehydrogenase

ECTree

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.1 With NAD+ or NADP+ as acceptor
                1.2.1.48 long-chain-aldehyde dehydrogenase

Engineering

Engineering on EC 1.2.1.48 - long-chain-aldehyde dehydrogenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C241S
site-directed mutagenesis, inactive active-site mutant
D245N
-
NAD+ cosubstrate binding is occuring but catalytic reduction is diminished
E207Q
site-directed mutagenesis, inactive mutant
E331Q
site-directed mutagenesis, inactive mutant
G185A
-
disruption of NAD+ binding/utilisation
G412R
-
disruption of interaction of side-chains with substrate
H411Y
-
disruption of the key abstraction of the hydroxyl hydrogen
N112A
site-directed mutagenesis, inactive mutant
Q445R
-
substitution in the recombinant protein
T184M
-
disruption of NAD+ binding/utilisation
T184R
-
disruption of NAD+ binding/utilisation
Y113F
site-directed mutagenesis, the mutant activity is unaltered compared to wild-type
Y410F
site-directed mutagenesis, the mutant shows normal Vmax/KM levels against octanal and dodecanal and a somewhat reduced but still considerable catalytic capacity for hexadecanal
C244S
-
the mutant shows about 90% reduction in catalytic efficiency with benzaldehyde and no activity with 4,4'-diapolycopendial compared to the wild type enzyme
F456A
-
the mutant shows about 50% reduction in catalytic efficiency with 4,4'-diapolycopendial compared to the wild type enzyme
F456A/F457A
-
the mutant shows about 15% reduction in catalytic efficiency with benzaldehyde and no activity with 4,4'-diapolycopendial compared to the wild type enzyme
F457A
-
the mutant shows about 40% reduction in catalytic efficiency with 4,4'-diapolycopendial compared to the wild type enzyme
K449E
-
the mutant shows slight reduction in catalytic efficiency with benzaldehyde and no activity with 4,4'-diapolycopendial compared to the wild type enzyme
Y92A
-
the mutant shows slight reduction in catalytic efficiency with benzaldehyde and no activity with 4,4'-diapolycopendial compared to the wild type enzyme