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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: γ-trimethylaminobutyraldehyde dehydrogenase

Gene: Aldh9a1 Accession Number: G-11009 (MetaCyc)

Synonyms: Aldehyde dehydrogenase family 9 member A1

Species: Rattus norvegicus

Summary:
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 1.2.1.19) 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].

Locations: cytosol

Map Position: [83,017,312 -> 83,034,047]

Molecular Weight of Polypeptide: 53.653 kD (from nucleotide sequence)

Unification Links: Entrez-gene:64040 , Mint:MINT-4580055 , PhosphoSite:Q9JLJ3 , Pride:Q9JLJ3 , Protein Model Portal:Q9JLJ3 , SMR:Q9JLJ3 , String:Q9JLJ3 , UniProt:Q9JLJ3

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

Gene-Reaction Schematic: ?

GO Terms:

Cellular Component: GO:0005829 - cytosol [Vaz00]

Credits:
Created 18-Nov-2008 by Fulcher CA , SRI International


Enzymatic reaction of: γ-trimethylaminobutyraldehyde dehydrogenase

Synonyms: 4-trimethylammoniobutyraldehyde dehydrogenase, 4-trimethylaminobutyraldehyde dehydrogenase, 4-N-trimethylaminobutyraldehyde dehydrogenase, 4-trimethylammoniobutanal:NAD+ 1-oxidoreductase

EC Number: 1.2.1.47

4-trimethylammoniobutanal + NAD+ + H2O <=> γ-butyrobetaine + NADH + 2 H+

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

Summary:
The enzyme was dependent on NAD+, which was greatly preferred over NADP+ [Vaz00].

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].

Kinetic Parameters:

Substrate
Km (μM)
Citations
4-trimethylammoniobutanal
1.4
[Vaz00]
NAD+
28.0
[Vaz00]


References

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

Vaz02: Vaz FM, Wanders RJ (2002). "Carnitine biosynthesis in mammals." Biochem J 361(Pt 3);417-29. PMID: 11802770


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Mon Nov 24, 2014, BIOCYC13B.