|Gene:||Aldh9a1||Accession Number: G-11009 (MetaCyc)|
Synonyms: Aldehyde dehydrogenase family 9 member A1
Species: Rattus norvegicus
The subunit structure of this enzyme from rat liver has not been reported.
This enzyme was purified from rat liver cytosol and recombinant enzyme was expressed in Escherichia coli. Its amino acid sequence was highly homologous to that of human aldehyde dehydrogenase 9 (EC 220.127.116.11) encoded by human gene ALDH9, which is thought to be the human γ-trimethylaminobutyraldehyde dehydrogenase ([Vaz00] and reviewed in [Vaz02]).
The enzyme has been found in rat liver, heart, kidney, muscle, brain and testis [vanVlies06].
|Map Position: [83,017,312 -> 83,034,047]|
Molecular Weight of Polypeptide: 53.653 kD (from nucleotide sequence)
Relationship Links: InterPro:IN-FAMILY:IPR015590 , InterPro:IN-FAMILY:IPR016160 , InterPro:IN-FAMILY:IPR016161 , InterPro:IN-FAMILY:IPR016162 , InterPro:IN-FAMILY:IPR016163 , Pfam:IN-FAMILY:PF00171 , Prosite:IN-FAMILY:PS00070 , Prosite:IN-FAMILY:PS00687
|Cellular Component:||GO:0005829 - cytosol [Vaz00]|
Enzymatic reaction of: γ-trimethylaminobutyraldehyde dehydrogenase
Synonyms: 4-trimethylammoniobutyraldehyde dehydrogenase, 4-trimethylaminobutyraldehyde dehydrogenase, 4-N-trimethylaminobutyraldehyde dehydrogenase, 4-trimethylammoniobutanal:NAD+ 1-oxidoreductase
EC Number: 18.104.22.168
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
The reaction is favored in the direction shown.
Alternative Substrates for 4-trimethylammoniobutanal: octanal [Vaz00 ] , palmitaldehyde [Vaz00 ] , hexanal [Vaz00 ] , heptanal [Vaz00 ] , betaine aldehyde [Vaz00 ] , acetaldehyde [Vaz00 ] , propanal [Vaz00 ] , butanal [Vaz00 ] , pentanal [Vaz00 ] , 4-aminobutanal [Vaz00 ]
In Pathways: L-carnitine biosynthesis
Recombinant enzyme was expressed as an MBP (maltose-binding protein) fusion protein and purified. Its substrate specificity and kinetic behavior was similar to that of the purified native enzyme, and to the recombinant human enzyme. Of the substrates tested, 4-trimethylammoniobutanal was preferred [Vaz00].
The Km values shown here are for the purified, native enzyme [Vaz00].
vanVlies06: van Vlies N, Wanders RJ, Vaz FM (2006). "Measurement of carnitine biosynthesis enzyme activities by tandem mass spectrometry: differences between the mouse and the rat." Anal Biochem 354(1);132-9. PMID: 16707092
Vaz00: Vaz FM, Fouchier SW, Ofman R, Sommer M, Wanders RJ (2000). "Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis." J Biol Chem 275(10);7390-4. PMID: 10702312
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