1.2.1.47: 4-trimethylammoniobutyraldehyde dehydrogenase
This is an abbreviated version!
For detailed information about 4-trimethylammoniobutyraldehyde dehydrogenase, go to the full flat file.
Word Map on EC 1.2.1.47
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1.2.1.47
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gamma-butyrobetaine
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proliferator-activated
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dioxygenase
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peroxisome
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l-carnitine
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polyunsaturated
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1.2.1.8
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badhs
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aldh4a1
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suckling
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gill
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betaine
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acetaldehyde
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trimethyllysine
- 1.2.1.47
- gamma-butyrobetaine
-
proliferator-activated
-
dioxygenase
- peroxisome
- l-carnitine
-
polyunsaturated
-
1.2.1.8
-
badhs
-
aldh4a1
-
suckling
-
gill
- betaine
- acetaldehyde
- trimethyllysine
Reaction
Synonyms
4-N-trimethylaminobutyraldehyde dehydrogenase, 4-N-trimethylaminobutyraldehyde dehydrogenase II, 4-trimethylaminobutyraldehyde dehydrogenase, 4-trimethylammoniobutyraldehyde dehydrogenase, aldehyde dehydrogenase 9A1, Aldh9a1, carnitine biosynthesis enzyme, dehydrogenase, trimethylaminobutyraldehyde, gamma-trimethylaminobutyraldehyde dehydrogenase, TMABA dehydrogenase, TMABA-DH, TMABADH, TMABAL dehydrogenase, TMABaldehyde-DH II, TMABALDH
ECTree
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Subunits
Subunits on EC 1.2.1.47 - 4-trimethylammoniobutyraldehyde dehydrogenase
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homotrimer
tetramer
trimer
additional information
4 * 56000, dimer-of-dimers, recombinant His-tagged enzyme, SDS-PAGE
tetramer
enzyme ALDH9A1 forms the classic ALDH superfamily dimer-of-dimers tetramer in solution. Analytical ultracentrifugation, small-angle X-ray scattering (SAXS), and negative stain electron microscopy are used for analysis
conformation of the inter-domain linker in the P1 ALDH9A1-NAD+ structure, modeling, overview. The in-solution quaternary structure of ALDH9A1 is determined using SAXS
additional information
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conformation of the inter-domain linker in the P1 ALDH9A1-NAD+ structure, modeling, overview. The in-solution quaternary structure of ALDH9A1 is determined using SAXS
additional information
each ALDH monomer displays a typical ALDHs fold composed of an oligomerization domain (residues 128-145 and 479-494), a coenzyme domain (residues 1-127, 146-257, 470-478), a catalytic domain (residues 258-448) with the catalytic Cys288, and an interdomain linker highly conserved in amino-acid sequence and folding. Nonetheless, structural comparison reveals a position and a unique fold of the interdomain linker of ALDH9A1. The oligomerization domain wraps over the groove between the catalytic and coenzyme domains of the other monomer forming the dimer
additional information
-
each ALDH monomer displays a typical ALDHs fold composed of an oligomerization domain (residues 128-145 and 479-494), a coenzyme domain (residues 1-127, 146-257, 470-478), a catalytic domain (residues 258-448) with the catalytic Cys288, and an interdomain linker highly conserved in amino-acid sequence and folding. Nonetheless, structural comparison reveals a position and a unique fold of the interdomain linker of ALDH9A1. The oligomerization domain wraps over the groove between the catalytic and coenzyme domains of the other monomer forming the dimer