Thirty-seven sets of crystallographic enzyme data were selected from Protein Data Bank (PDB, 1995). The average temperature factors (B) of the critical residues at the active site and the whole molecule of those enzymes were calculated respectively. The statistical results showed that the critical residues at the active site of most of the enzymes had lowerB factors than did the whole molecules, indicating that in the crystalline state the critical residues at the active site of the natural enzymes possess more stable conformation than do the whole molecules. The flexibility of the active site during the unfolding by denaturing was also discussed.
This is a preview of subscription content, log in to check access.
Buy single article
Instant access to the full article PDF.
Price includes VAT for USA
Tsou, C. L., Conformational flexibility of enzyme active site,Science, 1993, 262: 380.
Price, N. C., Sterens, L.,Fundamentals of Enzymelogy, Oxford: Oxford Univ. Press, 1982, 2.
Koshland, Jr. D. E., Application of a theory of enzyme specificity to protein synthesis,Proc. Natl. Acad. Sci., 1958, 44: 98.
Stryer, L.,Biochemistry, New York: Freeman, 1991, 119–120.
Horten, H. R., Moran, L. A., Ochs, R. S. et al.,Principles of Biochemistry, NJ: Neil Patterson Publishers/Prentice Hall, 1992, 124–125.
Jorgensen, A. M. M., Kristensen, S. M., Led, J. J. et al., Three-dimensional solution structure of an insulin dimer— A study of the B9 (Asp) mutant of human insulin using nuclear magnetic resonance, distance geometry and restrained molecular dynamics,J. Mol. Biol., 1992, 227: 1146.
Koshland, Jr. D. E., Role of flexibility in the specificity, control and evolution of enzymes,FEBS Lett., 1976, 62: E47.
Xie, G. F., Tsou, C. L., Conformational and activity changes during guanidinedenaturation of D-glyceraldehyde-3-phosphate dehydrogenase,Biochim. Biophys. Acta, 1987, 11: 19.
Zhou, H. M., Zhang, X. H., Yin, Y. et al., Conformational changes at the active site of creatine kinase at low concentrations of guanidium chloride,Biochem. J., 1993, 291: 103.
Frohlich, O., Jones, S. C., Denaturation of a membrane transport protein by urea,J. Mem. Biol., 1987, 98: 33.
Edwards, R. A., Jacobson, A. L., Huber, R. E., Thermal denaturation of u-galactosidase and of two site-specific mutants,Biochemistry, 1990, 29: 11001.
West, S. M., Kelly, S. M., Price, N. C. et al., The unfolding and attempted refolding of citrate synthetase from pig heart,Biochim. Biophys. Acta, 1990, 1037: 332.
Kelly, S. M., Price, N. C., The unfolding and refolding of pig heart fumarase,Biochem. J., 1991, 275: 745.
Rosi, G. L., Biological activity in the crystalline state,Cur. Op. SB., 1992, 2: 816.
Svergun, D. I., Barberato, C., Koch, M. H. J. et al., Large differences are observed between the crystal and solution quaternary structures of allosteric aspartate transcarbamylase in the R state,Protein SFG, 1997, 27: 110.
Bj is determined by the mass of atom and the working temperature.
About this article
Cite this article
Zhang, H., Song, S. & Lin, Z. CrystallographicB factor of critical residues at enzyme active site. Sci. China Ser. C.-Life Sci. 42, 225–232 (1999). https://doi.org/10.1007/BF03183597
- crystallographicB factor
- active site