Effect of enzyme processivity on the efficacy of a competitive chitinase inhibitor

Carbohydrate Polymers

Volumn 82, Issue 3, 2010, Pages 779-785

  Zakariassen, Henrik ^a   Klemetsen, Laila ^a   Sakuda, Shohei ^b   Vaaje Kolstad, Gustav ^a   Vrum, Kjell M ^c   Sørlie, Morten ^a   Eijsink, Vincent G H ^a  

^a NORWEGIAN UNIVERSITY OF LIFE SCIENCES   (Norway)

^b UNIVERSITY OF TOKYO   (Japan)

^c NORWEGIAN UNIVERSITY OF SCIENCE AND TECHNOLOGY   (Norway)

Author keywords

Chitin; Chitosan; Competitive inhibition; Glycoside hydrolase; Processivity

Indexed keywords

CHITINASES; COMPETITIVE INHIBITION; GLYCOSIDE HYDROLASES; LIGAND BINDING; NEGATIVE CORRELATION; PATHOGENIC ORGANISMS; PROCESSIVITY; SERRATIA; SERRATIA MARCESCENS; SUBSITES;

CATALYSTS; CHITIN; CHITOSAN; ENZYMES; PLANTS (BOTANY); SUGARS;

ENZYME INHIBITION;

FUNGI; HEXAPODA; NEMATODA; SERRATIA; SERRATIA MARCESCENS;

EID: 77955656597     PISSN: 01448617     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.carbpol.2010.05.051     Document Type: Article

References (53)

1. N.N. Aronson Jr., B.A. Halloran, M.F. Alexeyev, L. Amable, J.D. Madura, and L. Pasupulati Family 18 chitinase-oligosaccharide substrate interaction: Subsite preference and anomer selectivity of Serratia marcescens Biochemical Journal 376 2003 87 95
2. B.M.A. Banat, Y. Kameyama, T. Yoshioka, and D. Koga Purification and characterization of a 54 kDa chitinase from Bombyx mori Insect Biochemistry and Molecular Biology 29 1999 537 547
3. K. Bortone, A.F. Monzingo, S. Ernst, and J.D. Robertus The structure of an allosamidin complex with the Coccidioides immitis Chitinase defines a role for a second acid residue in substrate-assisted mechanism Journal of Molecular Biology 320 2002 293 302
4. M.B. Brurberg, V.G.H. Eijsink, A.J. Haandrikman, G. Venema, and I.F. Nes Chitinase B from Serratia marcescens BJL200 is exported to the periplasm without processing Microbiology 141 1995 123 131
5. M.B. Brurberg, V.G.H. Eijsink, and I.F. Nes Chararcterization of a chitinase gene (chiA) from Serratia marcescens BJL200 and one-step purification of the gene product FEMS Microbiology Letters 124 1994 399 404
6. M.B. Brurberg, I.F. Nes, and V.G.H. Eijsink Comparative studies of chitinase A and B from Serratia marcescens Microbiology 142 1996 1581 1589
7. B.T. Burlingham, and T.S. Widlanski An intuitive look at the relationship of Ki and IC50: A more general use for the Dixon plot Journal of Chemical Education 80 2003 214 218
8. A.P. Bussink, D. Speijer, J.M. Aerts, and R.G. Boot Evolution of mammalian chitinase(-like) members of family 18 glycosyl hydrolases Genetics 177 2007 959 970
9. 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
10. A. Chandumpai, N. Singhpibulporn, D. Faroongsarng, and P. Sornprasit Preparation and physico-chemical characterization of chitin and chitosan from the pens of the squid species, Loligo lessoniana and Loligo formosana Carbohydrate polymers 58 2004 467 474
11. G. Davies, and B. Henrissat Structures and mechanisms of glycosyl hydrolases Structure 3 1995 853 859
12. C. Divne, J. Sthlberg, T.T. Teeri, and T.A. Jones High-resolution crystal structures reveal how a cellulose chain is bound in the 50 long tunnel of cellobiohydrolase I from Trichoderma reesei Journal of Molecular Biology 275 1998 309 325
13. L.E. Donnelly, and P.J. Barnes Acidic mammalian chitinase - A potential target for asthma therapy Trends in Pharmacological Science 25 2004 509 511
14. K.I. Draget, K.M. Vrum, E. Moen, H. Gynnild, and O. Smidsrød Chitosan cross-linked with Mo(VI) polyoxyanions: A new gelling system Biomaterials 13 1992 635 638
15. V.G.H. Eijsink, G. Vaaje-Kolstad, K.M. Vrum, and S.J. Horn Towards new enzymes for biofuels: Lessons from chitinase research Trends in Biotechnology 26 2008 228 235
16. F. Fusetti, H. von Moeller, D. Houston, H.J. Rozeboom, B.W. Dijkstra, and R.G. Boot Structure of human chitotriosidase Journal of Biological Chemistry 277 2002 25537 25544
17. S.J. Horn, and V.G.H. Eijsink A reliable reducing end assay for chito-oligosaccharides Carbohydrate Polymers 56 2004 35 39
18. S.J. Horn, P. Sikorski, J.B. Cederkvist, G. Vaaje-Kolstad, M. Sørlie, and B. Synstad Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides Proceedings of the National Academy of Sciences USA 103 2006 18089 18094
19. S.J. Horn, A. Sørbotten, B. Synstad, P. Sikorski, M. Sørlie, and K.M. Vrum Endo/exo mechanism and processivity of family 18 chitinase produced by Serratia marcescens FEBS Journal 273 2006 491 503
20. S.J. Horn, M. Sørlie, G. Vaaje-Kolstad, A.L. Norberg, B. Synstad, and K.M. Vrum Comparative studies of chitinases A, B and C from Serratia marcescens Biocatalysis and Biotransformation 24 2006 39 53
21. E. Hult, F. Katouno, T.T. Uchiyama, and W.J. Sugiyama Molecular directionality in crystalline b-chitin: Hydrolysis by chitinase A and B from Serratia marcescens 2170 Biochemical Journal 388 2005 851 856
22. M. Jaworska, K. Sakurai, P. Gaudon, and E. Guibal Influence of chitosan characteristics on polymer properties. I. Crystallographic properties Polymer International 52 2003 198 205
23. V. Karlsen, E.B. Heggset, and M. Sørlie The use of isothermal titration calorimetry to determine the thermodynamics of metal ion binding to low-cost sorbents Thermochimica Acta 2010 10.1016/j.tca.2010.01.007
24. F. Katouno, M. Taguchi, K. Sakurai, T. Uchiyama, N. Nikiaidou, and T. Nonaka Importance of exposed aromatic residues in chitinase B from Serratia marcescens 2170 for crystalline chitin hydrolysis Journal of Biochemistry 136 2004 163 168
25. A. Koivula, T. Kinnari, V. Harjunpaa, L. Ruohonen, A. Teleman, and T. Drakenberg Tryptophan 272: An essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6A FEBS Letters 429 1998 341 346
26. J. Medve, J. Karlsson, D. Lee, and F. Tjerneld Hydrolysis of microcrystalline cellulose by cellobiohydrolase I and endoglucanase II from Trichoderma reesei: Adsorption, sugar production pattern, and synergism of the enzymes Biotechnology and Bioengineering 59 1998 621 634
27. A.M. Olland, J. Strand, E. Presman, R. Czerwinski, D. Joseph-McCarthy, and R. Krykbaev Triad of polar residues implicated in pH specificity of acidic mammalian chitinase Protein Science 18 2009 569 578
28. S. Pantoom, C. Songsiriritthigul, and W. Suginta The effects of the surface-exposed residues on the binding and hydrolytic activities of Vibrio carchariae chitinase A BMC Biochemistry 9 2008 2
29. Y. Papanikolau, G. Tavlas, C.E. Vorgias, and K. Petratos De novo purification scheme and crystallization conditions yield high-resolution structures of chitinase A and its complex with the inhibitor allosamidin Acta Crystallographica D59 2003 400 403
30. F.V. Rao, D.R. Houston, R.G. Boot, J.M.F.G. Aerts, S. Sakuda, and D.M.F. Van Aalten Crystal structures of allosamidin derivatives in complex with human nacrophage chitinase Journal of Biological Chemistry 278 2003 20110 20116
31. J. Rouvinen, T. Bergfors, T. Teeri, J.K. Knowles, and T.A. Jones Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei Science 249 1990 380 386
32. S. Sakuda, A. Isogai, S. Matsumoto, and A. Suzuki Search for microbial insect growth regulators. II. Allosamidin, a novel insect chitinase inhibitor The Journal of Antibiotics 40 1987 296 300
33. 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 Letters 27 1986 2475 2478
34. T. Sannan, K. Kurita, K. Ogura, and Y. Iwakura Studies on chitin: 7. I.r. spectroscopic determination of degree of deacetylation Polymer 19 1978 458 459
35. P. Sikorski, A. Sørbotten, S.J. Horn, V.G.H. Eijsink, and K.M. Vrum Serratia marcescens chitinases with tunnel-shaped substrate-binding grooves show endo activity and different degrees of processivity during enzymatic hydrolysis of chitosan Biochemistry 45 2006 9566 9574
36. M. Susana Cortizo, C.F. Berghoff, and J.L. Alessandrini Characterization of chitin from Illex argentinus squid pen Carbohydrate polymers 74 2008 10 15
37. A. Sørbotten, S.J. Horn, V.G.H. Eijsink, and K.M. Vrum Degradation of chitosan with chitinase B from Serratia marcescens. Production of chito-oligosaccharides and insight into enzyme processivity FEBS Journal 272 2005 538 549
38. T.T. Teeri Crystalline cellulose degradation: New insight into the function of cellobiohydrolases Trends in Biotechnology 15 1997 160 167
39. T.T. Teeri, A. Koivula, M. Linder, G. Wohlfahrt, C. Divne, and T.A. Jones Trichoderma reesei cellobiohydrolases: Why so efficient on crystalline cellulose? Biochemical Society Transactions 26 1998 173 178
40. 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
41. T. Uchiyama, F. Katouno, N. Nikaidou, T. Nonaka, J. Sugiyama, and T. Watanabe Roles of the exposed aromatic residues in crystalline chitin hydrolysis by chitinase A from Serratia marcescens 2170 Journal of Biological Chemistry 276 2001 41343 41349
42. M. van Eijk, C.P.A.A. van Roomen, G.H. Renkema, A.P. Bussink, L. Andrews, and E.F.C. Blommaart Characterization of human phagocyte-derived chitotriosidase, a component of innate immunity International Immunology 17 2005 1505 1512
43. 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 Proceedings of the National Academy of Sciences USA 98 2001 8979 8984
44. D.M.F. van Aalten, B. Synstad, M.B. Brurberg, E. Hough, B.W. Riise, and V.G.H. Eijsink Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9- resolution Proceedings of the National Academy of Sciences USA 97 2000 5842 5847
45. A. Varrot, T.P. Frandsen, I. von Ossowski, V. Boyer, S. Cottaz, and H. Driguez Structural basis for ligand binding and processivity in cellobiohydrolase Cel6A from Humicola insolens Structure 11 2003 855 864
46. I. von Ossowski, J. Sthlberg, A. Koivula, K. Piens, D. Becker, and H. Boer Engineering the exo-loop of Trichoderma reesei cellobiohydrolase, Cel7A. A comparison with Phanerochaete chrysosporium Cel7D Journal of Molecular Biology 333 2003 817 829
47. G. Vaaje-Kolstad, D.R. Houston, F.V. Rao, M.G. Peter, B. Synstad, and D.M.F. van Aalten Structure of the D142N mutant of the family 18 chitinase ChiB from Serratia marcescens and its complex with allosamidin Biochimica et Biophysica Acta 1696 2004 103 111
48. K.M. Vrum, M.W. Anthonsen, H. Grasdalen, and O. Smidsrød Determination of the degree of N-acetylation and the distribution of N-acetyl groups in partially N-deacetylated chitins (chitosans) by high-field n.m.r. spectroscopy Carbohydrate Research 211 1991 17 23
49. 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 Analytical Biochemistry 179 1989 131 137
50. H. Zakariassen, B.B. Aam, S.J. Horn, K.M. Varum, M. Sorlie, and V.G.H. Eijsink Aromatic residues in the catalytic center of chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency Journal of Biological Chemistry 284 2009 10610 10617
51. 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 Carbohydrate Polymers 81 2010 14 20
52. S. Zhang, and D.B. Wilson Surface residue mutations which change the substrate specificity of Thermomonospora fusca endoglucanase E2 Journal of Biotechnology 57 1997 101 113
53. Z. Zhu, T. Zheng, R.J. Homer, Y.K. Kim, N.Y. Chen, and L. Cohn Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation Science 304 2004 1678 1682