Entry - *602733 - ALDEHYDE DEHYDROGENASE, FAMILY 9, SUBFAMILY A, MEMBER 1; ALDH9A1 - OMIM
 
* 602733

ALDEHYDE DEHYDROGENASE, FAMILY 9, SUBFAMILY A, MEMBER 1; ALDH9A1


Alternative titles; symbols

ALDEHYDE DEHYDROGENASE 9; ALDH9
E3


HGNC Approved Gene Symbol: ALDH9A1

Cytogenetic location: 1q24.1     Genomic coordinates (GRCh38): 1:165,662,216-165,698,562 (from NCBI)


TEXT

Description

The aldehyde dehydrogenases (EC 1.2.1.3) are a family of isozymes that catalyze the oxidation of a broad range of aldehydes and the dehydrogenation of aldehyde metabolites of compounds such as corticosteroids and biogenic amines. The aldehyde dehydrogenase E3 catalyzes the dehydrogenation of gamma-aminobutyraldehyde to gamma-aminobutyric acid (GABA) (summary by Kurys et al., 1989).


Cloning and Expression

Kurys et al. (1989) identified a liver aldehyde dehydrogenase isozyme, which they called E3, that catalyzes the dehydrogenation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. By SDS-PAGE and gradient gel electrophoresis, they found that E3 is a tetramer of identical 54-kD subunits. Using antibodies against E3 to screen a liver cDNA library, Kurys et al. (1993) isolated partial E3 cDNAs.

Lin et al. (1996) isolated cDNAs containing the complete ALDH9 coding region, and found that the gene encodes a predicted 493-amino acid protein. These authors stated that their nucleotide sequence differs from that of Kurys et al. (1993) in 3 positions. By sequence analysis of the ALDH9 locus in several unrelated individuals, Lin et al. (1996) determined that 2 of the differences were due to polymorphism. They attributed the third difference to a misprint in Kurys et al. (1993). Northern blot analysis revealed that ALDH9 is expressed as a 2.4-kb mRNA in a variety of tissues, with the highest levels of expression in liver, skeletal muscle, and kidney.

To study the role of E3 in the synthesis of the central nervous system inhibitory neurotransmitter GABA, Kikonyogo and Pietruszko (1996) characterized the E3 expression pattern in brain. By Northern blot analysis, they found that E3 is expressed as a 2.9-kb mRNA in all regions of the brain, with the highest levels in the spinal cord.


Gene Structure

Lin et al. (1996) reported that the ALDH9 gene contains 10 exons and spans approximately 45 kb.


Mapping

By analysis of a somatic cell hybrid panel, McPherson et al. (1994) localized the E3 gene to chromosome 1. Using fluorescence in situ hybridization, Lin et al. (1996) mapped the ALDH9 gene to 1q22-q23.


Nomenclature

Vasiliou et al. (1999) discussed the eukaryotic aldehyde dehydrogenases, tabulated all known human polymorphisms, and recommended nomenclature based on divergent evolution and chromosomal mapping. They suggested that the symbol ALDH9 (the 'trivial' designation) be changed to ALDH9A1.


ALLELIC VARIANTS ( 1 Selected Example):

.0001 ALDH9A1*2 POLYMORPHISM

ALDH9A1, CYS115SER
  
RCV000007260

Lin et al. (1996) observed a polymorphism in exon 2 of the ALDH9 gene leading to a cys115-to-ser amino acid substitution. The wildtype allele was designated ALDH9A1*1 and the 115-ser allele was designated ALDH9A1*2.


REFERENCES

  1. Kikonyogo, A., Pietruszko, R. Aldehyde dehydrogenase from adult human brain that dehydrogenates gamma-aminobutyraldehyde: purification, characterization, cloning and distribution. Biochem. J. 316: 317-324, 1996. [PubMed: 8645224, related citations] [Full Text]

  2. Kurys, G., Ambroziak, W., Pietruszko, R. Human aldehyde dehydrogenase: purification and characterization of a third isozyme with low Km for gamma-aminobutyraldehyde. J. Biol. Chem. 264: 4715-4721, 1989. [PubMed: 2925663, related citations]

  3. Kurys, G., Shah, P. C., Kikonyogo, A., Reed, D., Ambroziak, W., Pietruszko, R. Human aldehyde dehydrogenase: cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde. Europ. J. Biochem. 218: 311-320, 1993. [PubMed: 8269919, related citations] [Full Text]

  4. Lin, S. W., Chen, J. C., Hsu, L. C., Hsieh, C.-L., Yoshida, A. Human gamma-aminobutyraldehyde dehydrogenase (ALDH9): cDNA sequence, genomic organization, polymorphism, chromosomal localization, and tissue expression. Genomics 34: 376-380, 1996. [PubMed: 8786138, related citations] [Full Text]

  5. McPherson, J. D., Wasmuth, J. J., Kurys, G., Pietruszko, R. Human aldehyde dehydrogenase: chromosomal assignment of the gene for the isozyme that metabolizes gamma-aminobutyraldehyde. Hum. Genet. 93: 211-212, 1994. [PubMed: 8112751, related citations] [Full Text]

  6. Vasiliou, V., Bairoch, A., Tipton, K. F., Nebert, D. W. Eukaryotic aldehyde dehydrogenase (ALDH) genes: human polymorphisms, and recommended nomenclature based on divergent evolution and chromosomal mapping. Pharmacogenetics 9: 421-434, 1999. [PubMed: 10780262, related citations]


Contributors:
Victor A. McKusick - updated : 11/4/1999
Creation Date:
Rebekah S. Rasooly : 6/19/1998
carol : 06/18/2012
carol : 6/12/2012
carol : 4/3/2001
carol : 4/3/2001
carol : 11/9/1999
terry : 11/4/1999
alopez : 6/19/1998

* 602733

ALDEHYDE DEHYDROGENASE, FAMILY 9, SUBFAMILY A, MEMBER 1; ALDH9A1


Alternative titles; symbols

ALDEHYDE DEHYDROGENASE 9; ALDH9
E3


HGNC Approved Gene Symbol: ALDH9A1

Cytogenetic location: 1q24.1     Genomic coordinates (GRCh38): 1:165,662,216-165,698,562 (from NCBI)


TEXT

Description

The aldehyde dehydrogenases (EC 1.2.1.3) are a family of isozymes that catalyze the oxidation of a broad range of aldehydes and the dehydrogenation of aldehyde metabolites of compounds such as corticosteroids and biogenic amines. The aldehyde dehydrogenase E3 catalyzes the dehydrogenation of gamma-aminobutyraldehyde to gamma-aminobutyric acid (GABA) (summary by Kurys et al., 1989).


Cloning and Expression

Kurys et al. (1989) identified a liver aldehyde dehydrogenase isozyme, which they called E3, that catalyzes the dehydrogenation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. By SDS-PAGE and gradient gel electrophoresis, they found that E3 is a tetramer of identical 54-kD subunits. Using antibodies against E3 to screen a liver cDNA library, Kurys et al. (1993) isolated partial E3 cDNAs.

Lin et al. (1996) isolated cDNAs containing the complete ALDH9 coding region, and found that the gene encodes a predicted 493-amino acid protein. These authors stated that their nucleotide sequence differs from that of Kurys et al. (1993) in 3 positions. By sequence analysis of the ALDH9 locus in several unrelated individuals, Lin et al. (1996) determined that 2 of the differences were due to polymorphism. They attributed the third difference to a misprint in Kurys et al. (1993). Northern blot analysis revealed that ALDH9 is expressed as a 2.4-kb mRNA in a variety of tissues, with the highest levels of expression in liver, skeletal muscle, and kidney.

To study the role of E3 in the synthesis of the central nervous system inhibitory neurotransmitter GABA, Kikonyogo and Pietruszko (1996) characterized the E3 expression pattern in brain. By Northern blot analysis, they found that E3 is expressed as a 2.9-kb mRNA in all regions of the brain, with the highest levels in the spinal cord.


Gene Structure

Lin et al. (1996) reported that the ALDH9 gene contains 10 exons and spans approximately 45 kb.


Mapping

By analysis of a somatic cell hybrid panel, McPherson et al. (1994) localized the E3 gene to chromosome 1. Using fluorescence in situ hybridization, Lin et al. (1996) mapped the ALDH9 gene to 1q22-q23.


Nomenclature

Vasiliou et al. (1999) discussed the eukaryotic aldehyde dehydrogenases, tabulated all known human polymorphisms, and recommended nomenclature based on divergent evolution and chromosomal mapping. They suggested that the symbol ALDH9 (the 'trivial' designation) be changed to ALDH9A1.


ALLELIC VARIANTS 1 Selected Example):

.0001   ALDH9A1*2 POLYMORPHISM

ALDH9A1, CYS115SER
SNP: rs121908986, gnomAD: rs121908986, ClinVar: RCV000007260

Lin et al. (1996) observed a polymorphism in exon 2 of the ALDH9 gene leading to a cys115-to-ser amino acid substitution. The wildtype allele was designated ALDH9A1*1 and the 115-ser allele was designated ALDH9A1*2.


REFERENCES

  1. Kikonyogo, A., Pietruszko, R. Aldehyde dehydrogenase from adult human brain that dehydrogenates gamma-aminobutyraldehyde: purification, characterization, cloning and distribution. Biochem. J. 316: 317-324, 1996. [PubMed: 8645224] [Full Text: https://doi.org/10.1042/bj3160317]

  2. Kurys, G., Ambroziak, W., Pietruszko, R. Human aldehyde dehydrogenase: purification and characterization of a third isozyme with low Km for gamma-aminobutyraldehyde. J. Biol. Chem. 264: 4715-4721, 1989. [PubMed: 2925663]

  3. Kurys, G., Shah, P. C., Kikonyogo, A., Reed, D., Ambroziak, W., Pietruszko, R. Human aldehyde dehydrogenase: cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde. Europ. J. Biochem. 218: 311-320, 1993. [PubMed: 8269919] [Full Text: https://doi.org/10.1111/j.1432-1033.1993.tb18379.x]

  4. Lin, S. W., Chen, J. C., Hsu, L. C., Hsieh, C.-L., Yoshida, A. Human gamma-aminobutyraldehyde dehydrogenase (ALDH9): cDNA sequence, genomic organization, polymorphism, chromosomal localization, and tissue expression. Genomics 34: 376-380, 1996. [PubMed: 8786138] [Full Text: https://doi.org/10.1006/geno.1996.0300]

  5. McPherson, J. D., Wasmuth, J. J., Kurys, G., Pietruszko, R. Human aldehyde dehydrogenase: chromosomal assignment of the gene for the isozyme that metabolizes gamma-aminobutyraldehyde. Hum. Genet. 93: 211-212, 1994. [PubMed: 8112751] [Full Text: https://doi.org/10.1007/BF00210615]

  6. Vasiliou, V., Bairoch, A., Tipton, K. F., Nebert, D. W. Eukaryotic aldehyde dehydrogenase (ALDH) genes: human polymorphisms, and recommended nomenclature based on divergent evolution and chromosomal mapping. Pharmacogenetics 9: 421-434, 1999. [PubMed: 10780262]


Contributors:
Victor A. McKusick - updated : 11/4/1999

Creation Date:
Rebekah S. Rasooly : 6/19/1998

Edit History:
carol : 06/18/2012
carol : 6/12/2012
carol : 4/3/2001
carol : 4/3/2001
carol : 11/9/1999
terry : 11/4/1999
alopez : 6/19/1998