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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Subunits
Subunits on EC 1.2.1.48 - long-chain-aldehyde dehydrogenase
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homodimer
octamer
tetramer
additional information
homodimer
human FALDH forms a symmetrical dimer. Each FALDH subunit in the asymmetric unit adopts the canonical aldehyde dehydrogenase fold, including an aminoterminal (N-terminal) cofactor-binding domain (residues 1-79 and 103-208), a catalytic domain (residues 209-419) and an oligomerization domain (residues 82-102 and 420-443) that connects the two subunits of the dimer, and the C-terminal residues 445-460 that form an alpha helix. The recombinant enzyme is truncated and lacks the predicted transmembrane alpha-helical region (residues 464-485) that is not included in the expression constructs, due to incompatibility with the protein production process
the dimeric FALDH displays a an element in its C-terminal region, a gatekeeper helix, which extends over the adjacent subunit, controlling the access to the substrate cavity and helping orientate both substrate cavities towards the membrane surface for efficient substrate transit between membranes and catalytic site. Three-dimensional structure analysis and modelling, overview
additional information
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the dimeric FALDH displays a an element in its C-terminal region, a gatekeeper helix, which extends over the adjacent subunit, controlling the access to the substrate cavity and helping orientate both substrate cavities towards the membrane surface for efficient substrate transit between membranes and catalytic site. Three-dimensional structure analysis and modelling, overview