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FBP1  -  fructose-1,6-bisphosphatase 1

Sus scrofa

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Disease relevance of FBP


High impact information on FBP


Chemical compound and disease context of FBP

  • Oxidation experiments using Escherichia coli thioredoxin, in analogy with the chloroplast FBPase system, indicate an unexpected mode of regulation for AF2372, a key phosphatase in this anaerobic sulfate reducer [6].
  • As estimated from enzymatic activity and visual inspection of coomassie blue-stained SDS-PAGE gels, porcine fructose-1,6-bisphosphatase constitutes as much as 20% of the soluble protein from the over-expressing E. coli strain [7].

Biological context of FBP


Anatomical context of FBP


Associations of FBP with chemical compounds


Regulatory relationships of FBP

  • Some aspects of the proposed model may be relevant to all forms of FBPase, including the thioredoxin-regulated FBPase from the chloroplast [21].

Analytical, diagnostic and therapeutic context of FBP


  1. Isolation and sequence analysis of the cDNA for pig kidney fructose 1,6-bisphosphatase. Williams, M.K., Kantrowitz, E.R. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  2. The form II fructose 1,6-bisphosphatase and phosphoribulokinase genes form part of a large operon in Rhodobacter sphaeroides: primary structure and insertional mutagenesis analysis. Gibson, J.L., Chen, J.H., Tower, P.A., Tabita, F.R. Biochemistry (1990) [Pubmed]
  3. Crystallographic evidence for the action of potassium, thallium, and lithium ions on fructose-1,6-bisphosphatase. Villeret, V., Huang, S., Fromm, H.J., Lipscomb, W.N. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  4. Crystal structure of the neutral form of fructose 1,6-bisphosphatase complexed with regulatory inhibitor fructose 2,6-bisphosphate at 2.6-A resolution. Liang, J.Y., Huang, S., Zhang, Y., Ke, H., Lipscomb, W.N. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  5. Molecular structure of fructose-1,6-bisphosphatase at 2.8-A resolution. Ke, H., Thorpe, C.M., Seaton, B.A., Marcus, F., Lipscomb, W.N. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  6. Unexpected similarity in regulation between an archaeal inositol monophosphatase/fructose bisphosphatase and chloroplast fructose bisphosphatase. Stieglitz, K.A., Seaton, B.A., Head, J.F., Stec, B., Roberts, M.F. Protein Sci. (2003) [Pubmed]
  7. High-level expression of porcine fructose-1,6-bisphosphatase in Escherichia coli: purification and characterization of the enzyme. Burton, V.A., Chen, M., Ong, W.C., Ling, T., Fromm, H.J., Stayton, M.M. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  8. Toward a mechanism for the allosteric transition of pig kidney fructose-1,6-bisphosphatase. Zhang, Y., Liang, J.Y., Huang, S., Lipscomb, W.N. J. Mol. Biol. (1994) [Pubmed]
  9. Decreased Fc and C3 receptor function in macrophage populations which are refractory to migration inhibitory factor, C3 activators, and immune complex. Leu, R.W., Hefley, S.M., Herriott, M.J. Cell. Immunol. (1983) [Pubmed]
  10. Role of microtubules in the regulation of metabolism in isolated cerebral microvessels. Lloyd, P.G., Hardin, C.D. Am. J. Physiol. (1999) [Pubmed]
  11. Complete amino acid sequence of pig kidney fructose-1,6-bisphosphatase. Marcus, F., Edelstein, I., Reardon, I., Heinrikson, R.L. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  12. Importance of the dimer-dimer interface for allosteric signal transduction and AMP cooperativity of pig kidney fructose-1,6-bisphosphatase. Site-specific mutagenesis studies of Glu-192 and Asp-187 residues on the 190's loop. Lu, G., Giroux, E.L., Kantrowitz, E.R. J. Biol. Chem. (1997) [Pubmed]
  13. Calcium inhibits muscle FBPase and affects its intracellular localization in cardiomyocytes. Gizak, A., Majkowski, M., Dus, D., Dzugaj, A. FEBS Lett. (2004) [Pubmed]
  14. Structure refinement of fructose-1,6-bisphosphatase and its fructose 2,6-bisphosphate complex at 2.8 A resolution. Ke, H.M., Thorpe, C.M., Seaton, B., Lipscomb, W.N., Marcus, F. J. Mol. Biol. (1990) [Pubmed]
  15. FBPase is in the nuclei of cardiomyocytes. Gizak, A., Dzugaj, A. FEBS Lett. (2003) [Pubmed]
  16. Lack of fructose-1,6-bisphosphatase activity in LLC-PK1 cells. Gstraunthaler, G., Pfaller, W., Kotanko, P. Am. J. Physiol. (1985) [Pubmed]
  17. Origin of cooperativity in the activation of fructose-1,6-bisphosphatase by Mg2+. Nelson, S.W., Honzatko, R.B., Fromm, H.J. J. Biol. Chem. (2004) [Pubmed]
  18. The influence of fructose-1:6-bisphosphate on the release of glycolytic enzymes from cellular structure. Nanhua, C., Nancarrow, D., Masters, C. Biochem. Int. (1986) [Pubmed]
  19. Identification of the highly reactive sulfhydryl group of pig kidney fructose 1,6-bisphosphatase at cysteine 128. Chatterjee, T., Edelstein, I., Marcus, F., Eby, J., Reardon, I., Heinrikson, R.L. J. Biol. Chem. (1984) [Pubmed]
  20. Selective thiol group modification renders fructose-1,6-bisphosphatase insensitive to fructose 2,6-bisphosphate inhibition. Reyes, A., Burgos, M.E., Hubert, E., Slebe, J.C. J. Biol. Chem. (1987) [Pubmed]
  21. The N-terminal segment of recombinant porcine fructose-1,6-bisphosphatase participates in the allosteric regulation of catalysis. Nelson, S.W., Kurbanov, F.T., Honzatko, R.B., Fromm, H.J. J. Biol. Chem. (2001) [Pubmed]
  22. Site-directed mutagenesis of residues at subunit interfaces of porcine fructose-1,6-bisphosphatase. Shyur, L.F., Aleshin, A.E., Honzatko, R.B., Fromm, H.J. J. Biol. Chem. (1996) [Pubmed]
  23. Glycine 122 is essential for cooperativity and binding of Mg2+ to porcine fructose-1,6-bisphosphatase. Zhang, R., Chen, L., Villeret, V., Fromm, H.J. J. Biol. Chem. (1995) [Pubmed]
  24. Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallography. Villeret, V., Huang, S., Zhang, Y., Lipscomb, W.N. Biochemistry (1995) [Pubmed]
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