Aldo-keto reductase family 1, member A1
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| Location (UCSC) | Chr 1: 45.55 – 45.57 Mb | Chr 4: 116.49 – 116.51 Mb | |||||||
| PubMed search | [3] | [4] | |||||||
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Alcohol dehydrogenase [NADP+] also known as aldehyde reductase or aldo-keto reductase family 1 member A1 is an
non-Hodgkin's lymphoma.[9]
Structure
Gene
The AKR1A1 gene lies on the
exons
.
Protein
AKR1A1 consists of 325
amino acids and weighs 36573Da. The tertiary structure consists of a beta/alpha-barrel, with the coenzyme-binding site located at the carboxy-terminus end of the strands of the barrel.[10] Alternative splicing of this gene results in two transcript variants encoding the same protein.[7]
Function
AKR1A1 gene is found highly expressed in kidney and liver, and moderately expressed in
4-hydroxynonenal and play a role in the resistance to oxidative stress.[16]
Clinical significance
A SNP in intron 5 of AKR1A1 has been found to be significantly associated with increased risk of non-Hodgkin's lymphoma.[9] AKR1A1 could activate procarcinogens, such as polycyclic aromatic hydrocarbon.[8] AKRs have been linked to metabolism of the anthracyclines doxorubicin (DOX) and daunorubicin (DAUN), allelic variants showed significantly reduced metabolic activities, and hence these allelic variants can possibly act as genetic biomarkers for the clinical development of DAUN-induced cardiotoxicity.[17]
Interactions
4-hydroxynonenal [16]
polycyclic aromatic hydrocarbon[8]
DAUN [17]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000117448 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028692 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- PMID 2498333.
- S2CID 34254843.
- ^ a b "Entrez Gene: AKR1A1 aldo-keto reductase family 1, member A1 (aldehyde reductase)".
- ^ PMID 11306097.
- ^ S2CID 11078978.
- PMID 15299353.
- ^ PMID 10510318.
- PMID 17537398.
- PMID 7766643.
- PMID 1748675.
- PMID 6753936.
- ^ PMID 23643085.
- ^ S2CID 14214962.
Further reading
- Dawson SJ, White LA (May 1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". The Journal of Infection. 24 (3): 317–20. PMID 1602151.
- Tanimoto T, Ohta M, Tanaka A, Ikemoto I, Machida T (1991). "Purification and characterization of human testis aldose and aldehyde reductase". The International Journal of Biochemistry. 23 (4): 421–8. PMID 1901806.
- Vander Jagt DL, Hunsaker LA, Robinson B, Stangebye LA, Deck LM (July 1990). "Aldehyde and aldose reductases from human placenta. Heterogeneous expression of multiple enzyme forms". The Journal of Biological Chemistry. 265 (19): 10912–8. PMID 2113526.
- Wermuth B, Omar A, Forster A, di Francesco C, Wolf M, von Wartburg JP, Bullock B, Gabbay KH (1987). "Primary structure of aldehyde reductase from human liver". Progress in Clinical and Biological Research. 232: 297–307. PMID 3615425.
- Barski OA, Gabbay KH, Grimshaw CE, Bohren KM (September 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, Fujii J, Wada Y, Taniguchi N (January 1995). "In vivo glycation of aldehyde reductase, a major 3-deoxyglucosone reducing enzyme: identification of glycation sites" (PDF). Biochemistry. 34 (4): 1433–8. PMID 7827091.
- Robinson B, Hunsaker LA, Stangebye LA, Vander Jagt DL (December 1993). "Aldose and aldehyde reductases from human kidney cortex and medulla". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1203 (2): 260–6. PMID 8268209.
- Sato S, Lin LR, Reddy VN, Kador PF (August 1993). "Aldose reductase in human retinal pigment epithelial cells". Experimental Eye Research. 57 (2): 235–41. PMID 8405190.
- Udovikova EA, Wojtczak L (May 1998). "Mitochondrial aldehyde reductase: identification and characterization in rat liver and kidney cortex". The International Journal of Biochemistry & Cell Biology. 30 (5): 597–608. PMID 9693960.
- Barski OA, Gabbay KH, Bohren KM (September 1999). "Characterization of the human aldehyde reductase gene and promoter". Genomics. 60 (2): 188–98. PMID 10486210.
- O'connor T, Ireland LS, Harrison DJ, Hayes JD (October 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". The Biochemical Journal. 343 Pt 2 (2): 487–504. PMID 10510318.
- Picklo MJ, Olson SJ, Markesbery WR, Montine TJ (July 2001). "Expression and activities of aldo-keto oxidoreductases in Alzheimer disease". Journal of Neuropathology and Experimental Neurology. 60 (7): 686–95. PMID 11444797.
- Laclau M, Lu F, MacDonald MJ (September 2001). "Enzymes in pancreatic islets that use NADP(H) as a cofactor including evidence for a plasma membrane aldehyde reductase". Molecular and Cellular Biochemistry. 225 (1–): 151–60. S2CID 38935230.
- Lehner B, Sanderson CM (July 2004). "A protein interaction framework for human mRNA degradation". Genome Research. 14 (7): 1315–23. PMID 15231747.
- El-Kabbani O, Green NC, Lin G, Carson M, Narayana SV, Moore KM, Flynn TG, DeLucas LJ (November 1994). "Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications". Acta Crystallographica Section D. 50 (Pt 6): 859–68. PMID 15299353.
- Bohren KM, Brownlee JM, Milne AC, Gabbay KH, Harrison DH (May 2005). "The structure of Apo R268A human aldose reductase: hinges and latches that control the kinetic mechanism". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1748 (2): 201–12. PMID 15769597.
External links
- AKR1A1 human gene location in the UCSC Genome Browser.
- AKR1A1 human gene details in the UCSC Genome Browser.
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