AKR1A1

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Aldo-keto reductase family 1, member A1 (aldehyde reductase)
PDB rendering based on 1ae4.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols AKR1A1 ; ALDR1; ALR; MGC12529; MGC1380
External IDs Template:OMIM5 Template:MGI HomoloGene74565
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Aldo-keto reductase family 1, member A1 (aldehyde reductase), also known as AKR1A1, is a human gene.[1]

This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. This member, also known as aldehyde reductase, is involved in the reduction of biogenic and xenobiotic aldehydes and is present in virtually every tissue. Alternative splicing of this gene results in two transcript variants encoding the same protein.[1]

References

  1. 1.0 1.1 "Entrez Gene: AKR1A1 aldo-keto reductase family 1, member A1 (aldehyde reductase)".

Further reading

  • Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. PMID 1602151.
  • Tanimoto T, Ohta M, Tanaka A; et al. (1991). "Purification and characterization of human testis aldose and aldehyde reductase". Int. J. Biochem. 23 (4): 421–8. PMID 1901806.
  • Vander Jagt DL, Hunsaker LA, Robinson B; et al. (1990). "Aldehyde and aldose reductases from human placenta. Heterogeneous expression of multiple enzyme forms". J. Biol. Chem. 265 (19): 10912–8. PMID 2113526.
  • Bohren KM, Bullock B, Wermuth B, Gabbay KH (1989). "The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases". J. Biol. Chem. 264 (16): 9547–51. PMID 2498333.
  • Wermuth B, Omar A, Forster A; et al. (1987). "Primary structure of aldehyde reductase from human liver". Prog. Clin. Biol. Res. 232: 297–307. PMID 3615425.
  • Barski OA, Gabbay KH, Grimshaw CE, Bohren KM (1995). "Mechanism of human aldehyde reductase: characterization of the active site pocket". Biochemistry. 34 (35): 11264–75. PMID 7669785.
  • Takahashi M, Lu YB, Myint T; et al. (1995). "In vivo glycation of aldehyde reductase, a major 3-deoxyglucosone reducing enzyme: identification of glycation sites". Biochemistry. 34 (4): 1433–8. PMID 7827091.
  • Robinson B, Hunsaker LA, Stangebye LA, Vander Jagt DL (1994). "Aldose and aldehyde reductases from human kidney cortex and medulla". Biochim. Biophys. Acta. 1203 (2): 260–6. PMID 8268209.
  • Sato S, Lin LR, Reddy VN, Kador PF (1993). "Aldose reductase in human retinal pigment epithelial cells". Exp. Eye Res. 57 (2): 235–41. doi:10.1006/exer.1993.1119. PMID 8405190.
  • Udovikova EA, Wojtczak L (1998). "Mitochondrial aldehyde reductase: identification and characterization in rat liver and kidney cortex". Int. J. Biochem. Cell Biol. 30 (5): 597–608. PMID 9693960.
  • Fujii J, Hamaoka R, Matsumoto A; et al. (1999). "The structural organization of the human aldehyde reductase gene, AKR1A1, and mapping to chromosome 1p33-->p32". Cytogenet. Cell Genet. 84 (3–4): 230–2. PMID 10393438.
  • Barski OA, Gabbay KH, Bohren KM (1999). "Characterization of the human aldehyde reductase gene and promoter". Genomics. 60 (2): 188–98. doi:10.1006/geno.1999.5915. PMID 10486210.
  • O'connor T, Ireland LS, Harrison DJ, Hayes JD (1999). "Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members". Biochem. J. 343 Pt 2: 487–504. PMID 10510318.
  • Picklo MJ, Olson SJ, Markesbery WR, Montine TJ (2001). "Expression and activities of aldo-keto oxidoreductases in Alzheimer disease". J. Neuropathol. Exp. Neurol. 60 (7): 686–95. PMID 11444797.
  • Laclau M, Lu F, MacDonald MJ (2002). "Enzymes in pancreatic islets that use NADP(H) as a cofactor including evidence for a plasma membrane aldehyde reductase". Mol. Cell. Biochem. 225 (1-): 151–60. PMID 11716357.
  • 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.
  • Lehner B, Sanderson CM (2004). "A protein interaction framework for human mRNA degradation". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMID 15231747.
  • El-Kabbani O, Green NC, Lin G; et al. (2005). "Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications". Acta Crystallogr. D Biol. Crystallogr. 50 (Pt 6): 859–68. doi:10.1107/S0907444994005275. PMID 15299353.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Bohren KM, Brownlee JM, Milne AC; et al. (2005). "The structure of Apo R268A human aldose reductase: hinges and latches that control the kinetic mechanism". Biochim. Biophys. Acta. 1748 (2): 201–12. doi:10.1016/j.bbapap.2005.01.006. PMID 15769597.

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