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Chemical Compound Review

Conduritol B     (1S,4S,5R,6R)-cyclohex-2-ene- 1,4,5,6-tetrol

Synonyms: CHEMBL73813, CHEBI:67224, AC1L231G, 25348-64-5, 138258-55-6, ...
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Disease relevance of Conduritol B

  • The variant GCases from Gaucher disease patients and selected variant GCases from the mouse had decreased relative k(cat) and differential effects on active site binding and/or attachment of mechanism-based covalent (conduritol B epoxide) or reversible (deoxynojirimycin derivatives) inhibitors [1].

High impact information on Conduritol B

  • To isolate and characterize the catalytic site of the normal enzyme, brominated 3H-labeled conduritol B epoxide (3H-Br-CBE), which inhibits the enzyme by binding covalently to this site, was used as an affinity label [2].
  • Here, we show that apoA-I-mediated cholesterol efflux was inhibited (by up to 53% over 8 h) when fibroblasts were treated with lactosylceramide or the glucocerebrosidase inhibitor conduritol B epoxide [3].
  • Human acid beta-glucosidase. Use of conduritol B epoxide derivatives to investigate the catalytically active normal and Gaucher disease enzymes [4].
  • These effectors also increased the reactivity of glucocerebrosidase to the inhibitor conduritol B epoxide; HSF alone had no effect (t1/2 = 19 +/- 0.5 min) whereas the maximum rate of inactivation (t1/2 = 4.0 min) by conduritol B epoxide was achieved in the presence of a mixture of PS (1 microgram) and HSF (3 micrograms) [5].
  • Cyclophellitol was shown to be more potent than conduritol B epoxide in inhibition of glucocerebrosidase and in induction of the neural abnormality [6].

Chemical compound and disease context of Conduritol B


Biological context of Conduritol B

  • Conduritol B epoxide did not protect GCase from the inhibition by these MCABs when covalently bound to the active site [8].
  • The procedure was also able to detect various specific effects: the inhibition of protein glycosylation with D-glucosamine and castanospermine, the inhibition of glycosphingolipid biosynthesis with L-cycloserine, and a slight enhancement of glycosphingolipid biosynthesis with conduritol B epoxide and castanospermine [9].
  • With regard to identifying carriers the bile salt dependent assay of Peters et al. and the conduritol B epoxide-dependent procedure gave the greatest discrimination between the mean beta-glucosidase values for the control and heterozygote samples when evaluated using Student's t test [10].
  • The most reliable assay for the identification of the carrier state was the conduritol B epoxide-dependent procedure which can be expected to provide the fewest false negative results when classifying heterozygotes (5%) [10].

Anatomical context of Conduritol B

  • The conduritol B epoxide-treated macrophages accumulated glucocerebroside as a function of time, progressing to a fivefold elevation over control values after 24 days of treatment [11].
  • Three fluorometric beta-glucosidase assays were compared for their ability to identify Gaucher's disease heterozygotes, using leukocytes as the source of enzyme: the pH 5.5-taurocholate assay of Peters et al.; the conduritol B epoxide dependent variation of that assay; and the newly developed method described herein [12].
  • To develop a model simulating this process, cultured murine peritoneal macrophages were treated with conduritol B epoxide, a specific irreversible inhibitor of acid beta-glucosidase, for 6, 15, and 24 days [11].

Associations of Conduritol B with other chemical compounds


Gene context of Conduritol B


Analytical, diagnostic and therapeutic context of Conduritol B


  1. Analyses of variant acid beta-glucosidases: effects of Gaucher disease mutations. Liou, B., Kazimierczuk, A., Zhang, M., Scott, C.R., Hegde, R.S., Grabowski, G.A. J. Biol. Chem. (2006) [Pubmed]
  2. Human acid beta-glucosidase: isolation and amino acid sequence of a peptide containing the catalytic site. Dinur, T., Osiecki, K.M., Legler, G., Gatt, S., Desnick, R.J., Grabowski, G.A. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  3. Glycosphingolipid accumulation inhibits cholesterol efflux via the ABCA1/apolipoprotein A-I pathway: 1-phenyl-2-decanoylamino-3-morpholino-1-propanol is a novel cholesterol efflux accelerator. Glaros, E.N., Kim, W.S., Quinn, C.M., Wong, J., Gelissen, I., Jessup, W., Garner, B. J. Biol. Chem. (2005) [Pubmed]
  4. Human acid beta-glucosidase. Use of conduritol B epoxide derivatives to investigate the catalytically active normal and Gaucher disease enzymes. Grabowski, G.A., Osiecki-Newman, K., Dinur, T., Fabbro, D., Legler, G., Gatt, S., Desnick, R.J. J. Biol. Chem. (1986) [Pubmed]
  5. Activators of spleen glucocerebrosidase from controls and patients with various forms of Gaucher's disease. Basu, A., Glew, R.H., Daniels, L.B., Clark, L.S. J. Biol. Chem. (1984) [Pubmed]
  6. Inhibition of glucocerebrosidase and induction of neural abnormality by cyclophellitol in mice. Atsumi, S., Nosaka, C., Iinuma, H., Umezawa, K. Arch. Biochem. Biophys. (1992) [Pubmed]
  7. Normalization of liver glucosylceramide levels in the "Gaucher" mouse by phosphatidylserine injection. Datta, S.C., Radin, N.S. Biochem. Biophys. Res. Commun. (1988) [Pubmed]
  8. Human acid beta-glucosidase. Use of inhibitory and activating monoclonal antibodies to investigate the enzyme's catalytic mechanism and saposin A and C binding sites. Fabbro, D., Grabowski, G.A. J. Biol. Chem. (1991) [Pubmed]
  9. Simultaneous determination of sugar incorporation into glycosphingolipids and glycoproteins. Paul, P., Bordmann, A., Rosenfelder, G., Towbin, H. Anal. Biochem. (1992) [Pubmed]
  10. An improved fluorometric leukocyte beta-glucosidase assay for Gaucher's disease. Daniels, L.B., Glew, R.H., Diven, W.F., Lee, R.E., Radin, N.S. Clin. Chim. Acta (1981) [Pubmed]
  11. Macrophages exposed in vitro to conduritol B epoxide resemble Gaucher cells. Newburg, D.S., Shea, T.B., Yatziv, S., Raghavan, S.S., McCluer, R.H. Exp. Mol. Pathol. (1988) [Pubmed]
  12. Use of 4-heptylumbelliferyl-beta-D-glucoside to identify Gaucher's disease heterozygotes. Butcher, B.A., Gopalan, V., Lee, R.E., Richards, T.C., Waggoner, A.S., Glew, R.H. Clin. Chim. Acta (1989) [Pubmed]
  13. Human lysosomal beta-glucosidase: kinetic characterization of the catalytic, aglycon, and hydrophobic binding sites. Grabowski, G.A., Gatt, S., Kruse, J., Desnick, R.J. Arch. Biochem. Biophys. (1984) [Pubmed]
  14. Glucosylceramide and the level of the glucosidase-stimulating proteins. Datta, S.C., Radin, N.S. Lipids (1986) [Pubmed]
  15. Distribution of conduritol B epoxide in the animal model for Gaucher's disease (Gaucher mouse). Stephens, M.C., Bernatsky, A., Singh, H., Kanfer, J.N., Legler, G. Biochim. Biophys. Acta (1981) [Pubmed]
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