Aldo-keto reductase family 1, member A1
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.
- ↑ 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.
- ↑ 3.0 3.1 "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. 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.
- 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.
- 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. doi:10.1021/bi00035a036. 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. doi:10.1021/bi00004a038. 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. doi:10.1016/0167-4838(93)90092-6. 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. 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.
- 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.
- 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. doi:10.1023/A:1012238709063. 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. PMC 139241. 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. 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.
- 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.
- 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.
External links
PDB gallery |
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| | 1ae4: ALDEHYDE REDUCTASE COMPLEXED WITH COFACTOR AND INHIBITOR, ALPHA CARBON ATOMS ONLY |
| 1cwn: CRYSTAL STRUCTURE OF PORCINE ALDEHYDE REDUCTASE HOLOENZYME |
| 1hqt: THE CRYSTAL STRUCTURE OF AN ALDEHYDE REDUCTASE Y50F MUTANT-NADP COMPLEX AND ITS IMPLICATIONS FOR SUBSTRATE BINDING |
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