Dissecting factors that contribute to ligand-binding energetics for family 18 chitinases

Thermochimica Acta

Volumn 511, Issue 1-2, 2010, Pages 189-193

  Norberg, Anne Line ^a   Eijsink, Vincent G H ^a   Sørlie, Morten ^a  

^a NORWEGIAN UNIVERSITY OF LIFE SCIENCES   (Norway)

Author keywords

Chitinase; Conformational changes; Inhibition; Isothermal titration calorimetry

Indexed keywords

BINDING ENERGETICS; BINDING PROCESS; CHITINASES; CONFORMATIONAL CHANGES; CONFORMATIONAL ENTROPY; EXPERIMENTAL ERRORS; INHIBITION; ISOTHERMAL TITRATION CALORIMETRY; LIGAND BINDING; N-ACETYLGLUCOSAMINE; POLYMERIC SUBSTRATE; SERRATIA MARCESCENS; SOLVATION ENTROPY; SUBSITES;

CALORIMETRY; ENTROPY; LIGANDS;

TITRATION;

EID: 78149282562     PISSN: 00406031     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tca.2010.08.013     Document Type: Article

References (34)

1. B. Henrissat, and G.J. Davies Structural and sequence-based classification of glycoside hydrolases Curr. Opin. Struct. Biol. 7 1997 637 644
2. F.H. Cederkvist, M.P. Parmer, K.M. Vrum, V.G.H. Eijsink, and M. Sørlie Inhibition of a family 18 chitinase by chitooligosaccharides Carbohydr. Polym. 74 2008 41 49
3. O.A. Andersen, A. Nathubhai, M.J. Dixon, I.M. Eggleston, and D.M. Van Aalten Structure-based dissection of the natural product cyclopentapeptide chitinase inhibitor argifin Chem. Biol. 15 2008 295 301
4. H. Izumida, M. Nishijima, T. Takadera, A.M. Nomoto, and H. Sano The effect of chitinase inhibitors, cyclo(Arg-Pro) against cell separation of Saccharomyces cerevisiae and the morphological change of Candida albicans J. Antibiot. (Tokyo) 49 1996 829 831
5. J. Saguez, F. Dubois, C. Vincent, J.C. Laberche, B.S. Sangwan-Norreel, and P. Giordanengo Differential aphicidal effects of chitinase inhibitors on the polyphagous homopteran Myzus persicae (Sulzer) Pest. Manage. Sci. 62 2006 1150 1154
6. L.E. Donnelly, and P.J. Barnes Acidic mammalian chitinase - a potential target for asthma therapy Trends Pharmacol. Sci. 25 2004 509 511
7. Z. Zhu, T. Zheng, R.J. Homer, Y.K. Kim, N.Y. Chen, L. Cohn, Q. Hamid, and J.A. Elias Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation Science 304 2004 1678 1682
8. E. Freire Do enthalpy and entropy distinguish first in class from best in class? Drug Discov. Today 13 2008 869 874
9. J.M. Macdonald, C.A. Tarling, E.J. Taylor, R.J. Dennis, D.S. Myers, S. Knapp, G.J. Davies, and S.G. Withers Chitinase inhibition by chitobiose and chitotriose thiazolines Angew. Chem. Int. Ed. Engl. 49 2010 2599 2602
10. G. Zolotnitsky, U. Cogan, N. Adir, V. Solomon, G. Shoham, and Y. Shoham Mapping glycoside hydrolase substrate subsites by isothermal titration calorimetry Proc. Natl. Acad. Sci. U.S.A. 101 2004 11275 11280
11. G.J. Davies, K.S. Wilson, and B. Henrissat Nomenclature for sugar-binding subsites in glycosyl hydrolases Biochem. J. 321 1997 557 559
12. S. Sakuda, A. Isogai, S. Matsumoto, A. Suzuki, and K. Koseki The structure of allosamidin, a novel insect chitinase inhibitor, produced by Streptomyces Sp Tetrahedron Lett. 27 1986 2475 2478
13. G. Vaaje-Kolstad, A. Vasella, M.G. Peter, C. Netter, D.R. Houston, B. Westereng, B. Synstad, V.G. Eijsink, and D.M. Van Aalten Interactions of a family 18 chitinase with the designedinhibitor HM508, and its degradation product,chitobiono-delta-lactone J. Biol. Chem. 2004
14. A.C. Terwisscha van Scheltinga, S. Armand, K.H. Kalk, A. Isogai, B. Henrissat, and B.W. Dijkstra Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis Biochemistry 34 1995 15619 15623
15. S.J. Horn, M. Sørlie, G. Vaaje-Kolstad, A.L. Norberg, B. Synstad, K.M. Vrum, and V.G.H. Eijsink Comparative studies of chitinases A, B and C from Serratia marcescens Biocatal. Biotransform. 24 2006 39 53
16. A. Perrakis, I. Tews, Z. Dauter, A.B. Oppenheim, I. Chet, K.S. Wilson, and C.E. Vorgias Crystal structure of a bacterial chitinase at 2.3 A resolution Structure 2 1994 1169 1180
17. D.M.F. van Aalten, B. Synstad, M.B. Brurberg, E. Hough, B.W. Riise, V.G.H. Eijsink, and R.K. Wierenga Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-angstrom resolution Proc. Natl. Acad. Sci. U.S.A. 97 2000 5842 5847
18. H. Zakariassen, B.B. Aam, S.J. Horn, K.M. Varum, M. Sorlie, and V.G. Eijsink Aromatic residues in the catalytic center of chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency J. Biol. Chem. 284 2009 10610 10617
19. M.B. Brurberg, I.F. Nes, and V.G.H. Eijsink Comparative studies of chitinases A and B from Serratia marcescens Microbiology 142 1996 1581 1589
20. B. Synstad, S. Gseidnes, D.M.F. van Aalten, G. Vriend, J.E. Nielsen, and V.G.H. Eijsink Mutational and computational analysis of the role of conserved residues in the active site of a family 18 chitinase Eur. J. Biochem. 271 2004 253 262
21. T. Wiseman, S. Williston, J.F. Brandts, and L.N. Lin Rapid measurement of binding constants and heats of binding using a new titration calorimeter Anal. Biochem. 179 1989 131 137
22. I.-M. Krokeide, B. Synstad, S. Gseidnes, S.J. Horn, V.G.H. Eijsink, and M. Sørlie Natural substrate assay for chitinases using high-performance liquid chromatography: a comparison with existing assays Anal. Biochem. 363 2007 128 134
23. F.H. Cederkvist, S.F. Saua, V. Karlsen, S. Sakuda, V.G.H. Eijsink, and M. Sørlie Thermodynamic analysis of allosamidin binding to a family 18 chitinase Biochemistry 46 2007 12347 12354
24. H. Zakariassen, and M. Sørlie Heat capacity changes in heme protein-ligand interactions Thermochim. Acta 464 2007 24 28
25. B.M. Baker, and K.P. Murphy Dissecting the energetics of a protein-protein interaction: the binding of ovomucoid third domain to elastase J. Mol. Biol. 268 1997 557 569
26. R.L. Baldwin Temperature dependence of the hydrophobic interaction in protein folding Proc. Natl. Acad. Sci. U.S.A. 83 1986 8069 8072
27. K.P. Murphy, P.L. Privalov, and S.J. Gill Common features of protein unfolding and dissolution of hydrophobic compounds Science 247 1990 559 561
28. K.P. Murphy Hydration and convergence temperatures - on the use and interpretation of correlation plots Biophys. Chem. 51 1994 311 326
29. J. Baban, S. Fjeld, S. Sakuda, V.G.H. Eijsink, and M. Sørlie The roles of three Serratia marcescens chitinases in chitin conversion are reflected in different thermodynamic signatures of allosamidin binding J. Phys. Chem. B 114 2010 6144 6149
30. R.G. Haverkamp, A.T. Marshall, and M.A.K. Williams Entropic and enthalpic contributions to the chair - boat conformational transformation in Dextran under single molecule stretching J. Phys. Chem. B 111 2007 13653 13657
31. D.M.F. van Aalten, D. Komander, B. Synstad, S. Gseidnes, M.G. Peter, and V.G.H. Eijsink Structural insights into the catalytic mechanism of a family 18 exo-chitinase Proc. Natl. Acad. Sci. U.S.A. 98 2001 8979 8984
32. Y. Papanikolau, G. Prag, G. Tavlas, C.E. Vorgias, A.B. Oppenheim, and K. Petratos High resolution structural analyses of mutant chitinase A complexes with substrates provide new insight into the mechanism of catalysis Biochemistry 40 2001 11338 11343
33. H. Zakariassen, V.G.H. Eijsink, and M. Sørlie Signatures of activation parameters reveal substrate-dependent rate determining steps in polysaccharide turnover by a family 18 chitinase Carbohydr. Polym. 81 2010 14 20
34. F. Fusetti, H. von Moeller, D. Houston, H.J. Rozeboom, B.W. Dijkstra, R.G. Boot, J.M.F.G. Aerts, and D.M.F. van Aalten Structure of human chitotriosidase. Implications for specific inhibitor design and function of mammalian chitinase-like lectins J. Biol. Chem. 277 2002 25537 25544