Aldo-keto reductase family 1, member A1

Template:PBB Alcohol dehydrogenase [NADP+] also known as aldehyde reductase or aldo-keto reductase family 1 member A1 is an enzyme that in humans is encoded by the AKR1A1 gene.^[1]^[2]^[3]

Function

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.^[3]

References

^ Bohren KM, Bullock B, Wermuth B, Gabbay KH (Jul 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.{{cite journal}}: CS1 maint: multiple names: authors list (link)
^ Fujii J, Hamaoka R, Matsumoto A, Fujii T, Yamaguchi Y, Egashira M, Miyoshi O, Niikawa N, Taniguchi N (Jul 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. doi:10.1159/000015265. PMID 10393438.{{cite journal}}: CS1 maint: multiple names: authors list (link)
^ ^a ^b "Entrez Gene: AKR1A1 aldo-keto reductase family 1, member A1 (aldehyde reductase)".

Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. 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. doi:10.1016/0020-711X(91)90169-N. PMID 1901806.{{cite journal}}: CS1 maint: multiple names: authors list (link)
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.{{cite journal}}: CS1 maint: multiple names: authors list (link)
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.{{cite journal}}: CS1 maint: multiple names: authors list (link)
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. doi:10.1021/bi00035a036. PMID 7669785.{{cite journal}}: CS1 maint: multiple names: authors list (link)
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. doi:10.1021/bi00004a038. PMID 7827091.{{cite journal}}: CS1 maint: multiple names: authors list (link)
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. doi:10.1016/0167-4838(93)90092-6. PMID 8268209.{{cite journal}}: CS1 maint: multiple names: authors list (link)
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.{{cite journal}}: CS1 maint: multiple names: authors list (link)
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. doi:10.1016/S1357-2725(97)00143-X. PMID 9693960.
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.{{cite journal}}: CS1 maint: multiple names: authors list (link)
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. doi:10.1042/0264-6021:3430487. PMC 1220579. PMID 10510318.{{cite journal}}: CS1 maint: multiple names: authors list (link)
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.{{cite journal}}: CS1 maint: multiple names: authors list (link)
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. doi:10.1023/A:1012238709063. PMID 11716357.{{cite journal}}: CS1 maint: multiple names: authors list (link)
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. PMC 139241. PMID 12477932.{{cite journal}}: CS1 maint: multiple names: authors list (link)
Lehner B, Sanderson CM (2004). "A protein interaction framework for human mRNA degradation". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. 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.{{cite journal}}: CS1 maint: multiple names: authors list (link)
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. PMC 528928. PMID 15489334.{{cite journal}}: CS1 maint: multiple names: authors list (link)
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.{{cite journal}}: CS1 maint: multiple names: authors list (link)

External links

AKR1A1 human gene location in the UCSC Genome Browser.
AKR1A1 human gene details in the UCSC Genome Browser.

This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by expanding it.

[pmid2498333-1] Bohren KM, Bullock B, Wermuth B, Gabbay KH (Jul 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.{{cite journal}}: CS1 maint: multiple names: authors list (link)

[pmid10393438-2] Fujii J, Hamaoka R, Matsumoto A, Fujii T, Yamaguchi Y, Egashira M, Miyoshi O, Niikawa N, Taniguchi N (Jul 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. doi:10.1159/000015265. PMID 10393438.{{cite journal}}: CS1 maint: multiple names: authors list (link)

[entrez-3] "Entrez Gene: AKR1A1 aldo-keto reductase family 1, member A1 (aldehyde reductase)".

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[2]

[3]

v t e Oxidoreductases: alcohol oxidoreductases (EC 1.1)
1.1.1: NAD/NADP acceptor	3-hydroxyacyl-CoA dehydrogenase 3-hydroxybutyryl-CoA dehydrogenase Alcohol dehydrogenase Aldo-keto reductase 1A1 1B1 1B10 1C1 1C3 1C4 7A2 Aldose reductase Beta-Ketoacyl ACP reductase Carbohydrate dehydrogenases Carnitine dehydrogenase D-malate dehydrogenase (decarboxylating) DXP reductoisomerase Glucose-6-phosphate dehydrogenase Glycerol-3-phosphate dehydrogenase HMG-CoA reductase IMP dehydrogenase Isocitrate dehydrogenase Lactate dehydrogenase L-threonine dehydrogenase L-xylulose reductase Malate dehydrogenase Malate dehydrogenase (decarboxylating) Malate dehydrogenase (NADP+) Malate dehydrogenase (oxaloacetate-decarboxylating) Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) Phosphogluconate dehydrogenase Sorbitol dehydrogenase Hydroxysteroid dehydrogenase: 3β 3β-HSD NSDHL 11β 11β-HSD1 11β-HSD2 17β
1.1.2: cytochrome acceptor	D-lactate dehydrogenase (cytochrome) D-lactate dehydrogenase (cytochrome c-553) Mannitol dehydrogenase (cytochrome)
1.1.3: oxygen acceptor	Glucose oxidase L-gulonolactone oxidase Xanthine oxidase Alcohol oxidase
1.1.4: disulfide as acceptor	Vitamin K epoxide reductase Vitamin-K-epoxide reductase (warfarin-insensitive)
1.1.5: quinone/similar acceptor	Malate dehydrogenase (quinone) Quinoprotein glucose dehydrogenase
1.1.99: other acceptors	Choline dehydrogenase L2HGDH

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Function

References

Further reading

External links