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Chemical Compound Review

AC1O4DFP     antimony hydroxide

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Disease relevance of antimony hydroxide


High impact information on antimony hydroxide

  • Fps1p has been shown to facilitate uptake of the metalloids arsenite and antimonite, and the Escherichia coli homolog, GlpF, facilitates the uptake and sensitivity to metalloid salts [6].
  • As(GS)(3) transport by MRP1 was osmotically sensitive and was inhibited by several conjugated organic anions (MRP1 substrates) as well as the metalloid antimonite (K(i) 2.8 microM) [7].
  • Antimonite elicits its effects by sequestering ArsA in the ArsA(1) conformation, which catalyzes rapid ATP hydrolysis at the A2 site to drive ArsA between conformations that have high (nucleotide-bound ArsA) and low affinity (nucleotide-free ArsA) for Sb(III) [8].
  • Overall, the results are consistent with PGPA being an intracellular ABC transporter that confers arsenite and antimonite resistance by sequestration of the metal-thiol conjugates [9].
  • On addition of antimonite, multisite catalysis involving both A1 and A2 sites occurs, resulting in a 40-fold increase in ATPase activity [10].

Chemical compound and disease context of antimony hydroxide


Biological context of antimony hydroxide


Anatomical context of antimony hydroxide


Associations of antimony hydroxide with other chemical compounds


Gene context of antimony hydroxide

  • Arsenite or antimonite allosterically activates the ArsA ATPase activity [20].
  • An internal deletion mutation in arsB resulted in decreased resistance to arsenate and total loss of arsenite and antimonite resistances [12].
  • Thus antimonite binding may act as a switch in regulating ATP binding to A2 and hence the ATPase activity of ArsA [14].
  • Extrapolation of the amount of FSBA required to inactivate the protein indicated that 1 mol of FSBA was sufficient to inhibit the activity of 1 mol of ArsA protein in the absence of substrates, while only 0.5 mol was required in the presence of the anionic substrate antimonite [17].
  • In the presence of antimonite or arsenite the ArsR protein is released from the operator/ promoter region of the ars operon and beta-galactosidase is expressed [21].


  1. Structure of the ArsA ATPase: the catalytic subunit of a heavy metal resistance pump. Zhou, T., Radaev, S., Rosen, B.P., Gatti, D.L. EMBO J. (2000) [Pubmed]
  2. The glycerol channel Fps1p mediates the uptake of arsenite and antimonite in Saccharomyces cerevisiae. Wysocki, R., Chéry, C.C., Wawrzycka, D., Van Hulle, M., Cornelis, R., Thevelein, J.M., Tamás, M.J. Mol. Microbiol. (2001) [Pubmed]
  3. Comparative genomic hybridization analysis of chromosomal changes occurring during development of acquired resistance to cisplatin in human ovarian carcinoma cells. Wasenius, V.M., Jekunen, A., Monni, O., Joensuu, H., Aebi, S., Howell, S.B., Knuutila, S. Genes Chromosomes Cancer (1997) [Pubmed]
  4. Arsenic sensing and resistance system in the cyanobacterium Synechocystis sp. strain PCC 6803. López-Maury, L., Florencio, F.J., Reyes, J.C. J. Bacteriol. (2003) [Pubmed]
  5. Influence of antimonite, selenite, and mercury on the toxicity of arsenite in primary rat hepatocytes. Hasgekar, N., Beck, J.P., Dunkelberg, H., Hirsch-Ernst, K.I., Gebel, T.W. Biological trace element research. (2006) [Pubmed]
  6. Arsenite transport by mammalian aquaglyceroporins AQP7 and AQP9. Liu, Z., Shen, J., Carbrey, J.M., Mukhopadhyay, R., Agre, P., Rosen, B.P. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  7. Arsenic transport by the human multidrug resistance protein 1 (MRP1/ABCC1). Evidence that a tri-glutathione conjugate is required. Leslie, E.M., Haimeur, A., Waalkes, M.P. J. Biol. Chem. (2004) [Pubmed]
  8. A kinetic model for the action of a resistance efflux pump. Walmsley, A.R., Zhou, T., Borges-Walmsley, M.I., Rosen, B.P. J. Biol. Chem. (2001) [Pubmed]
  9. The Leishmania ATP-binding cassette protein PGPA is an intracellular metal-thiol transporter ATPase. Légaré, D., Richard, D., Mukhopadhyay, R., Stierhof, Y.D., Rosen, B.P., Haimeur, A., Papadopoulou, B., Ouellette, M. J. Biol. Chem. (2001) [Pubmed]
  10. The anion-stimulated ATPase ArsA shows unisite and multisite catalytic activity. Kaur, P. J. Biol. Chem. (1999) [Pubmed]
  11. Asp45 is a Mg2+ ligand in the ArsA ATPase. Zhou, T., Rosen, B.P. J. Biol. Chem. (1999) [Pubmed]
  12. Regulation and expression of the arsenic resistance operon from Staphylococcus aureus plasmid pI258. Ji, G., Silver, S. J. Bacteriol. (1992) [Pubmed]
  13. Identification of a putative metal binding site in a new family of metalloregulatory proteins. Shi, W., Wu, J., Rosen, B.P. J. Biol. Chem. (1994) [Pubmed]
  14. Nucleotide binding to the C-terminal nucleotide binding domain of ArsA. Studies with an ATP analogue, 5'-p-fluorosulfonylbenzoyladenosine. Ramaswamy, S., Kaur, P. J. Biol. Chem. (1998) [Pubmed]
  15. Contribution of the Leishmania P-glycoprotein-related gene ltpgpA to oxyanion resistance. Papadopoulou, B., Roy, G., Dey, S., Rosen, B.P., Ouellette, M. J. Biol. Chem. (1994) [Pubmed]
  16. Antimonite regulation of the ATPase activity of ArsA, the catalytic subunit of the arsenical pump. Walmsley, A.R., Zhou, T., Borges-Walmsley, M.I., Rosen, B.P. Biochem. J. (2001) [Pubmed]
  17. Substrate-induced dimerization of the ArsA protein, the catalytic component of an anion-translocating ATPase. Ching, M.H., Kaur, P., Karkaria, C.E., Steiner, R.F., Rosen, B.P. J. Biol. Chem. (1991) [Pubmed]
  18. The role of arsenic-thiol interactions in metalloregulation of the ars operon. Shi, W., Dong, J., Scott, R.A., Ksenzenko, M.Y., Rosen, B.P. J. Biol. Chem. (1996) [Pubmed]
  19. Simultaneous determination of selenium and antimony compounds by capillary electrophoresis with indirect fluorescence detection. Chang, S.Y., Chiang, H.T. Electrophoresis (2002) [Pubmed]
  20. Genomic organization and chromosomal localization of the Asna1 gene, a mouse homologue of a bacterial arsenic-translocating ATPase gene. Bhattacharjee, H., Ho, Y.S., Rosen, B.P. Gene (2001) [Pubmed]
  21. Genetically engineered bacteria: electrochemical sensing systems for antimonite and arsenite. Scott, D.L., Ramanathan, S., Shi, W., Rosen, B.P., Daunert, S. Anal. Chem. (1997) [Pubmed]
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