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
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1.2.1.48
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sls
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ichthyosis
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spastic
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faldh
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aldh3a2
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neurocutaneous
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diplegia
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tetraplegia
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sjogren-larsson
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amadhs
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phytanic
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aminoaldehyde
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photophobia
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larsson
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quadriplegia
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alcohol:nad+
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glistening
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medicine
- 1.2.1.48
- sls
- ichthyosis
- spastic
- faldh
- aldh3a2
-
neurocutaneous
- diplegia
- tetraplegia
-
sjogren-larsson
- amadhs
-
phytanic
- aminoaldehyde
-
photophobia
-
larsson
- quadriplegia
-
alcohol:nad+
-
glistening
- medicine
Reaction
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
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Engineering
Engineering on EC 1.2.1.48 - long-chain-aldehyde dehydrogenase
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D245N
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NAD+ cosubstrate binding is occuring but catalytic reduction is diminished
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
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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
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the mutant shows about 50% reduction in catalytic efficiency with 4,4'-diapolycopendial compared to the wild type enzyme
F456A/F457A
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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
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the mutant shows about 40% reduction in catalytic efficiency with 4,4'-diapolycopendial compared to the wild type enzyme
K449E
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the mutant shows slight reduction in catalytic efficiency with benzaldehyde and no activity with 4,4'-diapolycopendial compared to the wild type enzyme
Y92A
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the mutant shows slight reduction in catalytic efficiency with benzaldehyde and no activity with 4,4'-diapolycopendial compared to the wild type enzyme