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Chemical Compound Review

AC1NTICF     (2E,6E,8E)-3,7-dimethyl-9- (2,6,6-trimethyl...

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Disease relevance of NSC122756

  • The simulations start from two simulated structures for the L550 intermediate of the photocycle, one involving a 13-cis retinal with strong torsions, the other a 13,14-dicis retinal, from which the M412 intermediate is initiated through proton transfer to Asp-85 [1].

High impact information on NSC122756

  • Human AR and HSI AR were very efficient in the reduction of all- trans -, 9- cis - and 13- cis -retinal ( k (cat)/ K (m)=1100-10300 mM(-1).min(-1)), constituting the first cytosolic NADP(H)-dependent retinal reductases described in humans [2].
  • We have previously characterized and cloned from kidney tissues the rat retinal dehydrogenase type 1 (RALDH1), which oxidizes all-trans and 9-cis retinal with high efficiency but is inactive with 13-cis retinal [3].
  • The enzyme, mouse retinal reductase (RRD, also known as human 2,4-dienoyl-CoA reductase), reduces all-trans-retinal [V(m) = 40 nmol min(-1) (mg of protein)(-1); K(0.5) = 2.3 microM] and has 4- and 60-fold less activity with 13-cis-retinal and 9-cis-retinal, respectively [4].
  • We arrived at the following explanation: The two bR isomers, one containing all-trans-retinal and the other 13-cis-retinal, respond differently to pH changes in the extravesicular and the intravesicular medium [5].
  • In the case of the monomer, the extent of light adaptation, i.e., the fraction of BR molecules containing 13-cis-retinal as chromophore which is converted by illumination to the respective pigment with the all-trans isomer, is reduced by 50% or more, and the rate of dark adaptation is slowed down about 2.5 times [6].

Biological context of NSC122756


Anatomical context of NSC122756


Associations of NSC122756 with other chemical compounds


Gene context of NSC122756


Analytical, diagnostic and therapeutic context of NSC122756

  • Based on the heavy-atom coordinates determined by the electron microscopy for the seven main helical regions of bacteriorhodopsin with the all-trans retinal isomer, energy optimizations were carried out for helix bundles containing the all-trans retinal and 13-cis retinal chromophores, respectively [13].
  • Analysis of retinal isomers with HPLC show that such an exposure produces a substance with 13-cis retinal as its chromophore and that it was significantly reduced after exposure to blue-green light [14].


  1. Molecular dynamics study of the M412 intermediate of bacteriorhodopsin. Xu, D., Sheves, M., Schulten, K. Biophys. J. (1995) [Pubmed]
  2. Human aldose reductase and human small intestine aldose reductase are efficient retinal reductases: consequences for retinoid metabolism. Crosas, B., Hyndman, D.J., Gallego, O., Martras, S., Parés, X., Flynn, T.G., Farrés, J. Biochem. J. (2003) [Pubmed]
  3. Cloning of monkey RALDH1 and characterization of retinoid metabolism in monkey kidney proximal tubule cells. Brodeur, H., Gagnon, I., Mader, S., Bhat, P.V. J. Lipid Res. (2003) [Pubmed]
  4. Reduction of all-trans-retinal in the mouse liver peroxisome fraction by the short-chain dehydrogenase/reductase RRD: induction by the PPAR alpha ligand clofibrate. Lei, Z., Chen, W., Zhang, M., Napoli, J.L. Biochemistry (2003) [Pubmed]
  5. Effect of a light-induced pH gradient on purple-to-blue and purple-to-red transitions of bacteriorhodopsin. Nasuda-Kouyama, A., Fukuda, K., Iio, T., Kouyama, T. Biochemistry (1990) [Pubmed]
  6. Photochemical cycle and light-dark adaptation of monomeric and aggregated bacteriorhodopsin in various lipid environments. Dencher, N.A., Kohl, K.D., Heyn, M.P. Biochemistry (1983) [Pubmed]
  7. Photoisomerization of the chromophore in bacteriorhodopsin during the proton pumping photocycle. Mowery, P.C., Stoeckenius, W. Biochemistry (1981) [Pubmed]
  8. Biotransformation of all-trans-retinal, 13-cis-retinal, and 9-cis-retinal catalyzed by conceptal cytosol and microsomes. Chen, H., Juchau, M.R. Biochem. Pharmacol. (1997) [Pubmed]
  9. The effects of vitamin A derivatives on in vitro antibody production by peripheral blood mononuclear cells (PBMC) from normal blood donors and patients with common variable immunodeficiency (CVID). Zhang, J.G., Morgan, L., Spickett, G.P. Clin. Exp. Immunol. (1997) [Pubmed]
  10. Photochemical cycle of bacteriorhodopsin studied by resonance Raman spectroscopy. Stockburger, M., Klusmann, W., Gattermann, H., Massig, G., Peters, R. Biochemistry (1979) [Pubmed]
  11. Kinetics and specificity of human liver aldehyde dehydrogenases toward aliphatic, aromatic, and fused polycyclic aldehydes. Klyosov, A.A. Biochemistry (1996) [Pubmed]
  12. Formation of 7-cis- and 13-cis-retinal pigments by irradiating squid rhodopsin. Maeda, A., Shichida, Y., Yoshizawa, T. Biochemistry (1979) [Pubmed]
  13. An energy-based approach to packing the 7-helix bundle of bacteriorhodopsin. Chou, K.C., Carlacci, L., Maggiora, G.M., Parodi, L.A., Schulz, M.W. Protein Sci. (1992) [Pubmed]
  14. A photoproduct with 13-cis retinal generated by irradiation with violet light in the octopus retina. Ohtsu, K., Kito, Y. Vision Res. (1985) [Pubmed]
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