Aldehyde dehydrogenase 9 family, member A1

Protein-coding gene in the species Homo sapiens
ALDH9A1
Identifiers
AliasesALDH9A1, ALDH4, ALDH7, ALDH9, E3, TMABADH, aldehyde dehydrogenase 9 family member A1, TMABA-DH, TMABALDH
External IDsOMIM: 602733; MGI: 1861622; HomoloGene: 55483; GeneCards: ALDH9A1; OMA:ALDH9A1 - orthologs
EC number1.2.1.3
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for ALDH9A1
Genomic location for ALDH9A1
Band1q24.1Start165,662,216 bp[1]
End165,698,562 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for ALDH9A1
Genomic location for ALDH9A1
Band1|1 H2.3Start167,177,560 bp[2]
End167,196,101 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right adrenal cortex

  • left adrenal gland

  • left adrenal cortex

  • salivary gland

  • minor salivary glands

  • mucosa of esophagus

  • left lobe of thyroid gland

  • right lobe of thyroid gland

  • liver

  • corpus callosum
Top expressed in
  • left lobe of liver

  • retinal pigment epithelium

  • Paneth cell

  • crypt of lieberkuhn of small intestine

  • human kidney

  • migratory enteric neural crest cell

  • ciliary body

  • jejunum

  • ileum

  • decidua
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • aldehyde dehydrogenase (NAD+) activity
  • oxidoreductase activity
  • aminobutyraldehyde dehydrogenase activity
  • 1-pyrroline dehydrogenase activity
  • 4-trimethylammoniobutyraldehyde dehydrogenase activity
  • 3-chloroallyl aldehyde dehydrogenase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
  • glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity
Cellular component
  • cytoplasm
  • extracellular exosome
  • cytosol
Biological process
  • cellular aldehyde metabolic process
  • hormone metabolic process
  • metabolism
  • neurotransmitter biosynthetic process
  • carnitine biosynthetic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

223

56752

Ensembl

ENSG00000143149

ENSMUSG00000026687

UniProt

P49189

Q9JLJ2

RefSeq (mRNA)

NM_000696
NM_001365774

NM_019993

RefSeq (protein)

NP_000687
NP_001352703

NP_064377
NP_001389759
NP_001389768
NP_001389769
NP_001389773

NP_001389774
NP_001389775
NP_001392024

Location (UCSC)Chr 1: 165.66 – 165.7 MbChr 1: 167.18 – 167.2 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

4-trimethylaminobutyraldehyde dehydrogenase is an enzyme that in humans is encoded by the ALDH9A1 gene.[5][6][7]

Function

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.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000143149 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026687 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ McPherson JD, Wasmuth JJ, Kurys G, Pietruszko R (February 1994). "Human aldehyde dehydrogenase: chromosomal assignment of the gene for the isozyme that metabolizes gamma-aminobutyraldehyde". Human Genetics. 93 (2): 211–2. doi:10.1007/bf00210615. PMID 8112751. S2CID 26773065.
  6. ^ Lin SW, Chen JC, Hsu LC, Hsieh CL, Yoshida A (June 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.
  7. ^ a b "Entrez Gene: ALDH9A1 aldehyde dehydrogenase 9 family, member A1".

External links

Further reading

  • Kurys G, Ambroziak W, Pietruszko R (March 1989). "Human aldehyde dehydrogenase. Purification and characterization of a third isozyme with low Km for gamma-aminobutyraldehyde". The Journal of Biological Chemistry. 264 (8): 4715–21. doi:10.1016/S0021-9258(18)83802-9. PMID 2925663.
  • Kurys G, Shah PC, Kikonygo A, Reed D, Ambroziak W, Pietruszko R (December 1993). "Human aldehyde dehydrogenase. cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde". European Journal of Biochemistry. 218 (2): 311–20. doi:10.1111/j.1432-1033.1993.tb18379.x. PMID 8269919.
  • Kikonyogo A, Pietruszko R (May 1996). "Aldehyde dehydrogenase from adult human brain that dehydrogenates gamma-aminobutyraldehyde: purification, characterization, cloning and distribution". The Biochemical Journal. 316 ( Pt 1) (1): 317–24. doi:10.1042/bj3160317. PMC 1217341. PMID 8645224.
  • Izaguirre G, Kikonyogo A, Pietruszko R (September 1997). "Tissue distribution of human aldehyde dehydrogenase E3 (ALDH9): comparison of enzyme activity with E3 protein and mRNA distribution". Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology. 118 (1): 59–64. doi:10.1016/s0305-0491(97)00022-9. PMID 9417993.
  • Vaz FM, Fouchier SW, Ofman R, Sommer M, Wanders RJ (March 2000). "Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis". The Journal of Biological Chemistry. 275 (10): 7390–4. doi:10.1074/jbc.275.10.7390. PMID 10702312.
  • Izaguirre G, Pietruszko R, Cho S, MacKerell A (December 2001). "Human aldehyde dehydrogenase catalytic activity and structural interactions with coenzyme analogs". Journal of Biomolecular Structure & Dynamics. 19 (3): 429–47. doi:10.1080/07391102.2001.10506752. PMID 11790142. S2CID 35621262.


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