AKR1B1

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Aldo-keto reductase family 1, member B1 (aldose reductase)
PDB rendering based on 1abn.
Available structures: 1abn, 1ads, 1az1, 1az2, 1ef3, 1el3, 1iei, 1mar, 1pwl, 1pwm, 1t40, 1t41, 1us0, 1x96, 1x97, 1x98, 1xgd, 1z3n, 1z89, 1z8a, 2acq, 2acr, 2acs, 2acu, 2agt, 2dux, 2duz, 2dv0, 2f2k, 2fz8, 2fz9, 2fzb, 2fzd, 2hv5, 2hvn, 2hvo, 2i16, 2i17, 2ikg, 2ikh, 2iki, 2ikj, 2ine, 2inz, 2ipw, 2iq0, 2iqd, 2is7, 2isf, 2j8t, 2nvc, 2nvd, 2pev, 2pf8, 2pfh
Identifiers
Symbol(s) AKR1B1; ADR; ALDR1; AR; MGC1804
External IDs OMIM: 103880 MGI: 1353494 HomoloGene: 68193
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 231 11677
Ensembl ENSG00000085662 ENSMUSG00000001642
Uniprot P15121 Q3TCL2
Refseq NM_001628 (mRNA)
NP_001619 (protein)		 NM_009658 (mRNA)
NP_033788 (protein)
Location Chr 7: 133.78 - 133.79 Mb Chr 6: 34.23 - 34.25 Mb
Pubmed search [1] [2]

Aldo-keto reductase family 1, member B1 (aldose reductase), also known as AKR1B1, 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 catalyzes the reduction of a number of aldehydes, including the aldehyde form of glucose, and is thereby implicated in the development of diabetic complications by catalyzing the reduction of glucose to sorbitol. There are a few putative pseudogenes for this gene, and one of them has been confirmed and mapped to chromosome 3.[1]

[edit] References

  1. ^ a b Entrez Gene: AKR1B1 aldo-keto reductase family 1, member B1 (aldose reductase).

[edit] Further reading

  • Borhani DW, Harter TM, Petrash JM (1992). "The crystal structure of the aldose reductase.NADPH binary complex.". J. Biol. Chem. 267 (34): 24841–7. PMID 1447221. 
  • Wilson DK, Bohren KM, Gabbay KH, Quiocho FA (1992). "An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications.". Science 257 (5066): 81–4. PMID 1621098. 
  • Graham A, Heath P, Morten JE, Markham AF (1991). "The human aldose reductase gene maps to chromosome region 7q35.". Hum. Genet. 86 (5): 509–14. PMID 1901827. 
  • Graham A, Brown L, Hedge PJ, et al. (1991). "Structure of the human aldose reductase gene.". J. Biol. Chem. 266 (11): 6872–7. PMID 1901857. 
  • Grundmann U, Bohn H, Obermeier R, Amann E (1990). "Cloning and prokaryotic expression of a biologically active human placental aldose reductase.". DNA Cell Biol. 9 (3): 149–57. PMID 2111143. 
  • Nishimura C, Matsuura Y, Kokai Y, et al. (1990). "Cloning and expression of human aldose reductase.". J. Biol. Chem. 265 (17): 9788–92. PMID 2112546. 
  • Morjana NA, Lyons C, Flynn TG (1989). "Aldose reductase from human psoas muscle. Affinity labeling of an active site lysine by pyridoxal 5'-phosphate and pyridoxal 5'-diphospho-5'-adenosine.". J. Biol. Chem. 264 (5): 2912–9. PMID 2492527. 
  • 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. 
  • Chung S, LaMendola J (1989). "Cloning and sequence determination of human placental aldose reductase gene.". J. Biol. Chem. 264 (25): 14775–7. PMID 2504709. 
  • Graham A, Hedge PJ, Powell SJ, et al. (1989). "Nucleotide sequence of cDNA for human aldose reductase.". Nucleic Acids Res. 17 (20): 8368. PMID 2510130. 
  • Akagi Y, Kador PF, Kuwabara T, Kinoshita JH (1984). "Aldose reductase localization in human retinal mural cells.". Invest. Ophthalmol. Vis. Sci. 24 (11): 1516–9. PMID 6417042. 
  • Ko BC, Lam KS, Wat NM, Chung SS (1995). "An (A-C)n dinucleotide repeat polymorphic marker at the 5' end of the aldose reductase gene is associated with early-onset diabetic retinopathy in NIDDM patients.". Diabetes 44 (7): 727–32. PMID 7789640. 
  • Wilson DK, Tarle I, Petrash JM, Quiocho FA (1993). "Refined 1.8 A structure of human aldose reductase complexed with the potent inhibitor zopolrestat.". Proc. Natl. Acad. Sci. U.S.A. 90 (21): 9847–51. PMID 8234324. 
  • Tarle I, Borhani DW, Wilson DK, et al. (1994). "Probing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110.". J. Biol. Chem. 268 (34): 25687–93. PMID 8245005. 
  • 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. 
  • Jaquinod M, Potier N, Klarskov K, et al. (1994). "Sequence of pig lens aldose reductase and electrospray mass spectrometry of non-covalent and covalent complexes.". Eur. J. Biochem. 218 (3): 893–903. PMID 8281941. 
  • Liu SQ, Bhatnagar A, Ansari NH, Srivastava SK (1993). "Identification of the reactive cysteine residue in human placenta aldose reductase.". Biochim. Biophys. Acta 1164 (3): 268–72. PMID 8343525. 
  • Nishimura C, Furue M, Ito T, et al. (1993). "Quantitative determination of human aldose reductase by enzyme-linked immunosorbent assay. Immunoassay of human aldose reductase.". Biochem. Pharmacol. 46 (1): 21–8. PMID 8347133. 
  • 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. 
  • Ferraretto A, Negri A, Giuliani A, et al. (1993). "Aldose reductase is involved in long-term adaptation of EUE cells to hyperosmotic stress.". Biochim. Biophys. Acta 1175 (3): 283–8. PMID 8435445. 
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