Environment of tryptophan 57 in porcine fructose-1,6-bisphosphatase studied by time-resolved fluorescence and site-directed mutagenesis

Photochemistry and Photobiology

Volumn 74, Issue 5, 2001, Pages 679-685

  Wen, Jin ^a   Nelson, Scott W ^a   Honzatko, Richard B ^a   Fromm, Herbert J ^a   Petrich, Jacob W ^a,b  

^a IOWA STATE UNIVERSITY   (United States)

^b 116 Gilman Hall ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; ASPARTIC ACID; FRUCTOSE BISPHOSPHATASE; TRYPTOPHAN;

AMINO ACID SUBSTITUTION; ARTICLE; CRYSTAL STRUCTURE; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME STRUCTURE; FLUORESCENCE; SITE DIRECTED MUTAGENESIS; SWINE;

AMINO ACID SUBSTITUTION; ANIMALS; ASPARAGINE; ASPARTIC ACID; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; FRUCTOSE-BISPHOSPHATASE; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN SUBUNITS; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; SWINE; TRYPTOPHAN;

SUIDAE; SUS SCROFA;

EID: 0035526570     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/0031-8655(2001)074<0679:EOTIPF>2.0.CO;2     Document Type: Article

References (31)

1. Benkovic, S. T. and M. M. de Maine (1982) Mechanism of action of fructose 1,6-bisphosphatase. Adv. Enzymol. Relat. Areas Mol. Biol. 53, 45-82.
2. Tejwani, G. A. (1983) Regulation of fructose-bisphosphatase activity. Adv. Enzymol. Relat. Areas Mol. Biol. 54, 121-194.
3. Pilkis, S. J., M. R. El-Maghrabi and T. H. Claus (1988) Hormonal regulation of hepatic gluconeogenesis and glycolysis. Annu. Rev. Biochem. 57, 755-783.
4. Pilkis, S. J., M. R. El-Maghrabi and T. H. Claus (1981) Inhibition of fructose-1,6-bisphosphatase by fructose 2,6-bisphosphate. J. Biol. Chem. 256, 3619-3622.
5. Van Schagtingen, E. and H. G. Hers (1981) Inhibition of fructose-1,6-bisphosphatase by fructose 2,6-bisphosphate. Proc. Natl. Acad. Sci. USA 78, 2861-2863.
6. Ke, H., Y. Zhang, J.-Y. Liang and W. N. Lipscomb (1991) Crystal structure of the neutral form of fructose-1,6-bisphosphatase complexed with the product fructose 6-phosphate at 2.1 Å resolution. Proc. Natl. Acad. Sci. USA 88, 2989-2993.
7. Nimmo, H. G. and K. F. Tipton (1975) The effect of pH on the kinetics of beef-liver fructose bisphosphatase. Eur. J. Biochem. 58, 567-574.
8. Liu, F. and H. J. Fromm (1988) Interaction of fructose 2,6-bisphosphate and AMP with fructose-1,6-bisphosphatase as studied by nuclear magnetic resonance spectroscopy. J. Biol. Chem. 263, 9122-9128.
9. Stone, S. R. and H. J. Fromm (1980) Investigations of the kinetic mechanism of bovine liver fructose 1,6-bisphosphatase. Biochemistry 19, 620-625.
10. Marcus, F., I. Edelstein, I. Reardon and R. L. Heinrikson (1982) Complete amino acid sequence of pig kidney fructose-1,6-bisphosphatase. Proc. Natl. Acad. Sci. USA 79, 7161-7165.
11. Zhang, Y., J.-Y. Liang, S. Huang and W. N. Lipscomb (1994) Toward a mechanism for the allosteric transition of pig kidney fructose-1,6-bisphosphatase. J. Mol. Biol. 244, 609-624.
12. Shyur, L.-F., A. E. Aleshin, R. B. Honzatko and H. J. Fromm (1996) Biochemical properties of mutant and wild-type fructose-1,6-bisphosphatases are consistent with the coupling of intra- and intersubunit conformational changes in the T- and R-state transition. J. Biol. Chem. 271, 33 301-33 307.
13. Ke, H., Y. Zhang, J.-Y. Liang and W. N. Lipscomb (1990) Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 6-phosphate, AMP, and magnesium. Proc. Natl. Acad. Sci. USA 87, 5243-5247.
14. 2+ at 2.0 Å resolution: aspects of synergism between Inhibitors. Proc. Natl. Acad. Sci. USA 91, 12 482-12 486.
15. Villeret, V., S. Huang, Y. Zhang and W. N. Lipscomb (1995) 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. Biochemistry 34, 4307-4315.
16. Choe, J.-Y., B. W. Poland, H. J. Fromm and R. B. Honzatko (1998) Role of a dynamic Loop in cation activation and allosteric regulation of recombinant porcine fructose-1,6-bisphosphatase. Biochemistry 37, 11 441-11 450.
17. Nelson, S. W., C. V. Iancu, J.-Y. Choe, R. B. Honzatko and H. J. Fromm (2000) Tryptophan fluorescence reveals the conformational state of a dynamic loop in recombinant porcine fructose-1,6-bisphosphatase. Biochemistry 39, 11 100-11 106.
18. Nelson, S. W., J.-Y. Choe, R. B. Honzatko and H. J. Fromm (2000) Mutations in the hinge of a dynamic loop broadly influence functional properties of fructose-1,6-bisphosphatase. J. Biol. Chem. 275, 29 986-29 992.
19. Choe, J.-Y., H. J. Fromm and R. B. Honzatko (2000) Crystal structures of fructose 1,6-bisphosphatase: mechanism of catalysis and allosteric inhibition revealed in product complexes. Biochemistry 39, 8565-8574.
20. Petrich, J. W., J. W. Longworth and G. R. Fleming (1987) Internal motion and electron transfer in proteins: a picosecond fluorescence study of three homologous azurins. Biochemistry 26, 2711-2722.
21. Smirnov, A. S., D. S. English, R. L. Rich, J. Lane, L. Teyton, A. W. Schwabacher, S. Luo, R. W. Thornburg and J. W. Petrich (1997) Photophysics and biological applications of 7-azaindole and its analogs. J. Phys. Chem. B 101, 2758.
22. Das, K., K. D. Ashby, A. V. Smirnov, F. C. Reinach, J. W. Petrich and C. S. Farah (1999) Fluorescence properties of recombinant tropomyosin containing tryptophan, 5-hydroxytryptophan, and 7-azatryptophan. Photochem. Photobiol. 70, 719.
23. Rich, R. L., A. V. Smirnov, A. W. Schwabacher and J. W. Petrich (1995) Synthesis and photophysics of the optical probe, N1-methyl-7-azatryptophan. J. Am. Chem. Soc. 117, 11 850.
24. Lakowicz, J. R. (1999) Principles of Fluorescence Spectroscopy, 2nd Ed. Kluwer Academic/Plenum Publishers, New York.
25. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
26. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-252.
27. Siano, D. B., J. W. Zyskind and H. J. Fromm (1975) A computer program for fitting and statistically analyzing initial rate data applied to bovine hexokinase type III isozyme. Arch. Biochem. Biophys. 319, 587-600.
28. Leatherbarrow, R. J. (1987) ENZFITTER: A Non-linear Regression Data Analysis Program for the IBM PC. Elsevier Science Publishers B. V., Amsterdam.
29. Lipari, G. and A. Szabo (1982) Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results. J. Am. Chem. Soc. 104, 4559-4570.
30. Callis, P. R. (1997) 1La and 1Lb transitions of tryptophan: applications of theory and experimental observations to fluorescence of proteins. Methods Enzymol. 278, 113-150.
31. Moncrieffe, M. C., N. Juranic, M. D. Kemple, J. D. Potter, S. Macura and F. G. Prendergast (2000) Structure-fluorescence correlations in a single tryptophan mutant of carp parvalbumin: solution structure, backbone and side-chain dynamics. J. Mol. Biol. 297, 147-163.