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
1.2.1.47 4-trimethylammoniobutyraldehyde dehydrogenaseAdvanced search results
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General Information on EC 1.2.1.47 - 4-trimethylammoniobutyraldehyde dehydrogenase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
aldehyde dehydrogenase 9A1 (ALDH9A1) belongs to the aldehyde dehydrogenase (ALDH) structural superfamily, which is a large group of enzymes that catalyze the NAD+-dependent oxidation of aldehydes to carboxylic acids. The superfamily comprises hundreds of distinct genes, including 19 ALDHs expressed in humans. ALDHs share a common protein fold and catalytic mechanism, but subtle differences in their active sites result in different preferences for the aldehyde substrate. Although ALDH9A1 exhibits the basic ALDH superfamily fold, the structure reveals two remarkable features. First, the final alpha-helix and beta-strand of the Rossmann dinucleotide-binding fold are disordered. Referred to as alphaE-betaE in the closely-related betaine ALDH, these secondary structural elements form extensive interactions with NAD+ in other ALDHs
malfunction
enzyme overexpression causes the Kawasaki disease (KD), an acute vasculitis that preferentially affects coronary arteries. The disease is still the leading cause of acquired heart disease in children. Patients suffering Kawasaki disease show increased TMABADH enzyme protein levels compared to controls
metabolism
the enzyme is involved in the carnitine synthesis pathway, it is abundantly expressed in tissues showing high rates of beta-oxidation such as liver and kidney
physiological function
the major in vivo function of this enzyme is to catalyze the penultimate step of carnitine biosynthesis, the oxidation of TMBAL to 4-N-trimethylaminobutyrate. Carnitine functions in the transport of long-chain fatty acids from the cytosol to the mitochondrial matrix for the synthesis of acyl-CoAs for beta-oxidation. ALDH9A1 functions indirectly in beta-oxidation
additional information
additional information
structure analysis, overview. Structural comparison reveals a position and a unique fold of the interdomain linker of ALDH9A1. This unique difference is not compatible with the presence of a bound substrate and a large conformational rearrangement of the linker up to 30 A has to occur to allow the access of the substrate channel. Moreover, the alphabetaE region consisting of an alpha-helix and a beta-strand of the coenzyme domain at the dimer interface are disordered, likely due to the loss of interactions with the inter-domain linker, which leads to incomplete beta-nicotinamide adenine dinucleotide (NAD+) binding pocket
additional information
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structure analysis, overview. Structural comparison reveals a position and a unique fold of the interdomain linker of ALDH9A1. This unique difference is not compatible with the presence of a bound substrate and a large conformational rearrangement of the linker up to 30 A has to occur to allow the access of the substrate channel. Moreover, the alphabetaE region consisting of an alpha-helix and a beta-strand of the coenzyme domain at the dimer interface are disordered, likely due to the loss of interactions with the inter-domain linker, which leads to incomplete beta-nicotinamide adenine dinucleotide (NAD+) binding pocket
additional information
the active conformation of the enzyme, in which the Rossmann dinucleotide-binding domain is fully ordered and the inter-domain linker adopts the canonical beta-hairpin observed in other ALDH structures. The presence of an aldehyde substrate and NAD+ promotes isomerization of the enzyme into the active conformation
additional information
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the active conformation of the enzyme, in which the Rossmann dinucleotide-binding domain is fully ordered and the inter-domain linker adopts the canonical beta-hairpin observed in other ALDH structures. The presence of an aldehyde substrate and NAD+ promotes isomerization of the enzyme into the active conformation
