ALDH9A1

From Wikipedia, the free encyclopedia


Aldehyde dehydrogenase 9 family, member A1
Identifiers
Symbol(s) ALDH9A1; ALDH4; ALDH7; ALDH9; E3; TMABADH
External IDs OMIM: 602733 MGI1861622 HomoloGene55483
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 223 56752
Ensembl ENSG00000143149 ENSMUSG00000026687
Uniprot P49189 Q3TG52
Refseq NM_000696 (mRNA)
NP_000687 (protein)
XM_991914 (mRNA)
XP_997008 (protein)
Location Chr 1: 163.9 - 163.93 Mb Chr 1: 169.19 - 169.2 Mb
Pubmed search [1] [2]

Aldehyde dehydrogenase 9 family, member A1, also known as ALDH9A1, is a human gene.[1]

This protein belongs to the aldehyde dehydrogenase family of proteins. It has a high activity for oxidation of gamma-aminobutyraldehyde and other amino aldehydes. The enzyme catalyzes the dehydrogenation of gamma-aminobutyraldehyde to gamma-aminobutyric acid (GABA). This isozyme is a tetramer of identical 54-kD subunits.[1]

[edit] References

[edit] Further reading

  • Kurys G, Ambroziak W, Pietruszko R (1989). "Human aldehyde dehydrogenase. Purification and characterization of a third isozyme with low Km for gamma-aminobutyraldehyde.". J. Biol. Chem. 264 (8): 4715-21. PMID 2925663. 
  • McPherson JD, Wasmuth JJ, Kurys G, Pietruszko R (1994). "Human aldehyde dehydrogenase: chromosomal assignment of the gene for the isozyme that metabolizes gamma-aminobutyraldehyde.". Hum. Genet. 93 (2): 211-2. PMID 8112751. 
  • Kurys G, Shah PC, Kikonygo A, et al. (1994). "Human aldehyde dehydrogenase. cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde.". Eur. J. Biochem. 218 (2): 311-20. PMID 8269919. 
  • Kikonyogo A, Pietruszko R (1996). "Aldehyde dehydrogenase from adult human brain that dehydrogenates gamma-aminobutyraldehyde: purification, characterization, cloning and distribution.". Biochem. J. 316 ( Pt 1): 317-24. PMID 8645224. 
  • Lin SW, Chen JC, Hsu LC, et al. (1996). "Human gamma-aminobutyraldehyde dehydrogenase (ALDH9): cDNA sequence, genomic organization, polymorphism, chromosomal localization, and tissue expression.". Genomics 34 (3): 376-80. doi:10.1006/geno.1996.0300. PMID 8786138. 
  • Izaguirre G, Kikonyogo A, Pietruszko R (1998). "Tissue distribution of human aldehyde dehydrogenase E3 (ALDH9): comparison of enzyme activity with E3 protein and mRNA distribution.". Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 118 (1): 59-64. PMID 9417993. 
  • Vaz FM, Fouchier SW, Ofman R, et al. (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. 
  • Izaguirre G, Pietruszko R, Cho S, MacKerell A (2002). "Human aldehyde dehydrogenase catalytic activity and structural interactions with coenzyme analogs.". J. Biomol. Struct. Dyn. 19 (3): 429-47. PMID 11790142. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1.". Nature 441 (7091): 315-21. doi:10.1038/nature04727. PMID 16710414.