Glu 69 is essential for the high sensitivity of muscle fructose-1,6-bisphosphatase inhibition by calcium ions

FEBS Letters

Volumn 581, Issue 7, 2007, Pages 1347-1350

  Zarzycki, Marek ^a   Maciaszczyk, Ewa ^a   Dzugaj, Andrzej ^a  

^a UNIVERSITY OF WROC AW   (Poland)

Author keywords

Calcium; Glyconeogenesis; Muscle fructose 1,6 bisphosphatase; Site directed mutagenesis

Indexed keywords

ADENOSINE PHOSPHATE; CALCIUM ION; FRUCTOSE BISPHOSPHATASE; GLUTAMIC ACID; GLUTAMINE; ISOENZYME; LIVER ENZYME; LYSINE; MUSCLE ENZYME;

ALLOSTERISM; ARTICLE; CHEMICAL MODIFICATION; ENZYME INHIBITION; FEASIBILITY STUDY; GLUCONEOGENESIS; MUTATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; SITE DIRECTED MUTAGENESIS;

ADENOSINE MONOPHOSPHATE; AMINO ACID SUBSTITUTION; ANIMALS; CALCIUM; CATIONS, DIVALENT; FRUCTOSE-BISPHOSPHATASE; GLUTAMIC ACID; GLUTAMINE; MUSCLE, SKELETAL; POINT MUTATION; RABBITS;

EID: 33947369488     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.02.051     Document Type: Article

References (24)

1. Benkovic S.J., and deMaine M.M. Mechanism of action of fructose 1,6-bisphosphatase. Adv. Enzymol. Relat. Area Mol. Biol. 53 (1982) 45-82
2. Tejwani G.A. Regulation of fructose-bisphosphatase activity. Adv. Enzymol. Relat. Area Mol. Biol. 54 (1983) 121-194
3. Dzugaj A. Localization and regulation of muscle fructose-1,6-bisphosphatase, the key enzyme of glyconeogenesis. Adv. Enzyme Regul. 46 (2006) 51-71
4. Pilkis S.J., El-Maghrabi M.R., Pilkis J., and Claus T. Inhibition of fructose-1,6-bisphosphatase by fructose 2,6-bisphosphate. J. Biol. Chem. 256 (1981) 3619-3622
5. Van Schaftingen E., and Hers H.G. Inhibition of fructose-1,6-bisphosphatase by fructose-2,6-bisphosphate. Proc. Natl. Acad. Sci. USA 78 (1981) 2861-2863
6. Skałecki K., Mularczyk W., and Dzugaj A. Kinetic properties of d-fructose-1,6-bisphosphate 1-phosphohydrolase isolated from human muscle. Biochem. J. 310 (1995) 1029-1035
7. Tillmann H., and Eschrich K. Isolation and characterization of an allelic cDNA for human muscle fructose-1,6-bisphosphatase. Gene 212 (1998) 295-304
8. Ke H.M., Liang J.Y., Zhang Y.P., and Lipscomb W.N. Conformational transition of fructose-1,6-bisphosphatase: structure comparison between the AMP complex (T form) and the fructose 6-phosphate complex (R form). Biochemistry 30 (1991) 4412-4420
9. Villeret V., Huang S., Fromm H.J., and Lipscomb W.N. Crystallographic evidence for the action of potassium, thallium, and lithium ions on fructose-1,6-bisphosphatase. Proc. Natl. Acad. Sci. USA 92 (1995) 8916-8920
10. Zhang Y., Liang J.-Y., Huang S., and Lipscomb W.N. Toward a mechanism for the allosteric transition of pig kidney fructose-1,6-bisphosphatase. J. Mol. Biol. 244 (1994) 609-624
11. Choe J.Y., Poland B.W., Fromm H.J., and Honzatko R.B. Role of a dynamic loop in cation activation and allosteric regulation of recombinant porcine fructose-1,6-bisphosphatase. Biochemistry 37 (1998) 11441-11450
12. Zhu D.W., Xu G.J., Rehse P.H., Shi R., Zhao F.K., and Lin S.X. Crystallization and preliminary crystallographic data of fructose-1,6-bisphosphatase from human muscle. Acta. Crystallogr. D Biol. Crystallogr. 57 (2001) 847-849
13. Gizak A., Majkowski M., Dus D., and Dzugaj A. Calcium inhibits muscle FBPase and affects its intracellular localization in cardiomyocytes. FEBS Lett. 576 (2004) 445-448
14. Mamczur P., Rakus D., Gizak A., Dus D., and Dzugaj A. The effect of calcium ions on subcellular localization of aldolase-FBPase complex in skeletal muscle. FEBS Lett. 579 (2005) 1607-1612
15. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
16. Rakus D., and Dzugaj A. Muscle aldolase decreases muscle FBPase sensitivity toward AMP inhibition. Biochem. Biophys. Res. Commun. 275 (2000) 611-616
17. Leatherbarrow, R.J. (1992). GraFit Version 3.0, Erithacus Software, Staines, UK.
18. Goding J.W. Conjugation of antibodies with fluorochromes: modifications to the standard methods. J. Immunol. Methods 13 (1976) 215-226
19. Rakus D., Tillmann H., Wysocki R., Ułaszewski S., Eschrich K., and Dzugaj A. Different sensitivities of mutants and chimeric forms of human muscle and liver fructose-1,6-bisphosphatases towards AMP. Biol. Chem. 384 (2003) 51-58
20. Van Tol A., Black W.J., and Horecker B.L. Activation of rabbit muscle fructose diphosphatase by EDTA and the effect of divalent cations. Arch. Biochem. Biophys. 151 (1972) 591-596
21. Dzugaj A., Chu D.K., El-Dorry H.A., and Horecker B.L. Isolation of the S-peptide formed on digestion of fructose 1,6-bisphosphatase with subtilisin and its non-covalent association with the enzyme protein. Biochem. Biophys. Res. Commun. 70 (1976) 638-646
22. MacGregor J.S., Hannappel E., Xu G.J., Pontremoli S., and Horecker B.L. Conservation of primary structure at the proteinase-sensitive site of fructose 1,6-bisphosphatases. Arch. Biochem. Biophys. 217 (1982) 652-664
23. Choe J.Y., Fromm H.J., and Honzatko R.B. Crystal structures of fructose 1,6-bisphosphatase: mechanism of catalysis and allosteric inhibition revealed in product complexes. Biochemistry 39 (2000) 8565-8574
24. Choe J.Y., Nelson S.W., Fromm H.J., and Honzatko R.B. Interaction of Tl+ with product complexes of fructose-1,6-bisphosphatase. J. Biol. Chem. 278 (2003) 16008-16014