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Gene Review

AKR1A1  -  aldo-keto reductase family 1, member A1...

Sus scrofa

Synonyms: ALR1, Akr1a4
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High impact information on ALR1


Biological context of ALR1


Anatomical context of ALR1


Associations of ALR1 with chemical compounds


Physical interactions of ALR1


Other interactions of ALR1

  • Both ALR1 and ALR2 may be involved in the reduction of isocorticosteroids [5].

Analytical, diagnostic and therapeutic context of ALR1


  1. Structure of porcine aldehyde reductase holoenzyme. el-Kabbani, O., Judge, K., Ginell, S.L., Myles, D.A., DeLucas, L.J., Flynn, T.G. Nat. Struct. Biol. (1995) [Pubmed]
  2. A mitochondrial NADP+-dependent reductase related to the 4-aminobutyrate shunt. Purification, characterization, and mechanism. Hearl, W.G., Churchich, J.E. J. Biol. Chem. (1985) [Pubmed]
  3. A functional arginine residue in NADPH-dependent aldehyde reductase from pig kidney. Davidson, W.S., Flynn, T.G. J. Biol. Chem. (1979) [Pubmed]
  4. Kinetics and mechanism of action of aldehyde reductase from pig kidney. Davidson, W.S., Flynn, T.G. Biochem. J. (1979) [Pubmed]
  5. Identification of pig brain aldehyde reductases with the high-Km aldehyde reductase, the low-Km aldehyde reductase and aldose reductase, carbonyl reductase, and succinic semialdehyde reductase. Cromlish, J.A., Flynn, T.G. J. Neurochem. (1985) [Pubmed]
  6. Some properties of pig kidney-cortex aldehyde reductase. Morpeth, F.F., Dickinson, F.M. Biochem. J. (1980) [Pubmed]
  7. Kinetic mechanism of sheep liver NADPH-dependent aldehyde reductase. De Jongh, K.S., Schofield, P.J., Edwards, M.R. Biochem. J. (1987) [Pubmed]
  8. Aldose and aldehyde reductase in animal tissues. Flynn, T.G. Metab. Clin. Exp. (1986) [Pubmed]
  9. Properties of the nicotinamide adenine dinucleotide phosphate-dependent aldehyde reductase from pig kidney. Amino acid composition, reactivity of cysteinyl residues, and stereochemistry of D-glyceraldehyde reduction. Flynn, T.G., Shires, J., Walton, D.J. J. Biol. Chem. (1975) [Pubmed]
  10. Structure of aldehyde reductase holoenzyme in complex with the potent aldose reductase inhibitor fidarestat: implications for inhibitor binding and selectivity. El-Kabbani, O., Carbone, V., Darmanin, C., Oka, M., Mitschler, A., Podjarny, A., Schulze-Briese, C., Chung, R.P. J. Med. Chem. (2005) [Pubmed]
  11. Crystal structure of an aldehyde reductase Y50F mutant-NADP complex and its implications for substrate binding. Ye, Q., Hyndman, D., Green, N., Li, X., Korithoski, B., Jia, Z., Flynn, T.G. Proteins (2001) [Pubmed]
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