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Biochemistry (Moscow)

, Volume 67, Issue 8, pp 850–871 | Cite as

The Structure and Mechanism of Action of Cellulolytic Enzymes

  • M. L. RabinovichEmail author
  • M. S. Melnick
  • A. V. Bolobova
Article

Abstract

The modern structural classification of polysaccharases comprising cellulase–hemicellulase enzyme systems is dis cussed. Their catalytic domains are currently grouped into 15 of more than 80 known glycosyl hydrolase families, whereas substrate binding domains fall into 13 families. The structures of catalytic and substrate binding domains, as well as linker sequences, are briefly considered. A hypothetical mechanism of concerted action of catalytic and substrate binding domains of cellobiohydrolases on the surface of highly ordered cellulose is suggested.

glycosyl hydrolase families cellulases xylanases endoglucanases cellobiohydrolases catalytic domains cellulose binding domains 

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REFERENCES

  1. 1.
    Henrissat, B. (1997) Mol. Microbiol., 23, 848–849.Google Scholar
  2. 2.
    Nutt, A., Sild, V., and Petterson, G. (1998) Eur. J. Biochem., 259, 200–206.Google Scholar
  3. 3.
    Kubicek, C. P. (1992) Adv. Biochem. Eng. Biotechnol. (Fiechter, A., ed.) Vol. 45, Springer-Verlag, Berlin-Heidelberg, pp. 1–27.Google Scholar
  4. 4.
    Tomme, P., Warren, R. A. J., and Gilkes, N. R. (1995) Adv. Microb. Physiol., 37, 1–81. Google Scholar
  5. 5.
    Bennett, N. A., Ryan, J., Biely, P., Vrsanska, M., Kremnicky, L., Macris, B. J., Kekos, D., Christakopoulos, P., Katapodis, P., Claeyssens, M., Nerinckx, W., Ntauma, P., and Bhat, M. K. (1998) Carbohydr. Res., 306, 445–455.Google Scholar
  6. 6.
    Beguin, P. (1990) Annu. Rev. Microbiol., 44, 219–265.Google Scholar
  7. 7.
    Beguin, P., and Alzari, P. M. (1998) Biochem. Soc. Trans., 26, 178–185.Google Scholar
  8. 8.
    Gilkes, N. R., Henrissat, B., and Kilburn, D. G. (1991) Microbiol. Rev., 55, 303–315.Google Scholar
  9. 9.
    Henrissat, B., and Bairoch, A. (1996) Biochem. J., 316, 722–726. Google Scholar
  10. 10.
    Rabinovich, M. L., and Melnick, M. S. (2000) Advances in Biological Chemistry [in Russian], Vol. 40, ONTI PNTs RAN, Pushchino, pp. 205–266.Google Scholar
  11. 11.
    Rodionova, N. A. (1989) Advances in Science and Technology. Biotechnology [in Russian], Vol. 19, VINITI, Moscow.Google Scholar
  12. 12.
    Sinitsyn, A. P., Gusakov A. V., and Chernoglazov, V. M. (1995) Bioconversion of Lignocellulose Materials [in Russian], Moscow State University Publishers, Moscow.Google Scholar
  13. 13.
    Beguin, P., and Aubert, J.-P. (1994) FEMS Microbiol. Rev., 13, 25–58.Google Scholar
  14. 14.
    Bolobova, A. V., and Kurakov, A. V. (1999) Prikl. Biokhim. Mikrobiol., 35, 402–408.Google Scholar
  15. 15.
    Kurakov, A. V., and Bolobova, A. V. (1999) Prikl. Biokhim. Mikrobiol., 35, 332–341.Google Scholar
  16. 16.
    Erikson, K.-E., Blanchette, R. A., and Ander, P. (1990) Microbial and Enzymatic Degradation of Wood and Wood Components, Springer Verlag, Berlin-Heidelberg, Germany.Google Scholar
  17. 17.
    Henrissat, B., Claeyssens, M., Tomme, P., Lemesle, L., and Mornon, J.-P. (1989) Gene, 81, 83–92.Google Scholar
  18. 18.
    Himmel, M. E., Karplus, P. A., Sakon, J., Adney, W. S., Baker, J. O., and Thomas, S. R. (1997) Appl. Biochem. Biotechnol., 63–65, 315–325.Google Scholar
  19. 19.
    Chen, H., Li, X. L., Blum, D. L., and Ljungdahl, L. G. (1998) FEMS Microbiol. Lett., 159, 63–68.Google Scholar
  20. 20.
    Juy, M., Amit, A. G., Alzari, P. M., Poljak, R. J., Claeyssens, M., Beguin, P., and Aubert, J.-P. (1992) Nature, 357, 89–91.Google Scholar
  21. 21.
    Rouvinen, J., Bergfors, T., Teeri, T., Knowles, J. K. C., and Jones, T. A. (1990) Science, 249, 380–386.Google Scholar
  22. 22.
    Tavares, G. A., Beguin, P., and Alzari, P. M. (1997) J. Mol. Biol., 273, 701–713.Google Scholar
  23. 23.
    Derewenda, U., Swenson, L., Green, R., Wei, Y., Morosoli, R., Shareck, F., Kluepfel, D., and Derewenda, Z. S. (1994) J. Biol. Chem., 269, 20811–20819.Google Scholar
  24. 24.
    Roig, V., Fierbode, H.-P., Ducros, V., Czjzek, M., Belaich, A., Gaudin, C., Belaich, J.-P., and Haser, R. (1993) J. Mol. Biol., 223, 325–330.Google Scholar
  25. 25.
    Sakon, J., Adney, W. S., Himmel, M. E., Thomas, S. R., and Karplus, P. A. (1996) Biochemistry, 35, 10648–10660.Google Scholar
  26. 26.
    Spezio, M., Wilson, D. B., and Karplus, P. A. (1993) Biochemistry, 32, 9906–9916.Google Scholar
  27. 27.
    Spezio, M., Irwin, D., Karplus, P. A., Zhang, S., Taylor, J., and Wilson, D. B. (1993) Genetics, Biochemistry and Ecology of Lignocellulose Degradation (Shimada, K., and Ohmiya, K., eds.) Uni Publishers, Tokyo, pp. 308–317.Google Scholar
  28. 28.
    Divne, C., Stahlberg, J., Reinikainen, T., Ruohonen, L., Pettersson, G., Knowles, J. K. C., Teeri, T. T., and Jones, T. A. (1994) Science, 265, 524–530.Google Scholar
  29. 29.
    Davies, G., Tolley, S., Wilson, K., Schulein, M., and Dodson, G. (1992) J. Mol. Biol., 228, 970–972.Google Scholar
  30. 30.
    Parsiegla, G., Juy, M., Reverbel-Leroy, C., Tardif, C., Belaich, J. P., Driguez, H., and Haser, R. (1998) EMBO J., 17, 5551–5562.Google Scholar
  31. 31.
    Irwin, D., Shin, D. H., Zhang, S., Barr, B. K., Sakon, J., Karplus, P. A., and Wilson, D. B. (1998) J. Bacteriol., 180, 1709–1714.Google Scholar
  32. 32.
    Dominguez, R., Souchon, H., and Alzari, P. M. (1994) Proteins: Structure, Function and Genetics, 19, 158–163.Google Scholar
  33. 33.
    Souchon, H., Spinelli, S., Beguin, P., and Alzari, P. M. (1994) J. Mol. Biol., 255, 1348–1356.Google Scholar
  34. 34.
    White, A., Withers, S. G., Gilkes, N. R., and Rose, D. R. (1994) Biochemistry, 33, 12546–12554.Google Scholar
  35. 35.
    Arase, A., Yomo, T., Urabe, I., Hata Y., Katsube, Y., and Okada, H. (1993) FEBS Lett., 316, 123–127.Google Scholar
  36. 36.
    Torronen, A., and Rouvinen, J. (1995) Biochemistry, 34, 847–855.Google Scholar
  37. 37.
    Okada, H. (1991) Microbial Utilization of Renewable Resources (Kinoshila, S., and Bhumiratana, A., eds.) International Center of Cooperative Research in Biotechnology, Japan, pp. 1–7.Google Scholar
  38. 38.
    Ward, M., Wu, S., Dauberman, J., Weiss, G., Larenas, E., Bower, B., Rey, M., Oarkson, K., and Bott, R. (1993) Trichoderma reesei Cellulases and Other Hydrolases (Suominen, P., and Reinikainen, T., eds.) Foundation for Biotechnical and Industrial Fermentation Research, Helsinki, pp. 153–158.Google Scholar
  39. 39.
    Davies, G. J., Dodson, G. G., Hubbard, R. E., Tolley, S. P., Dauter, Z., Wilson, K. S., Hjort, C., Mikkelsen, M. J., Rasmussen, G., and Schulein, M. (1993) Nature, 365, 362–366.Google Scholar
  40. 40.
    Parsiegla, G., Juy, M., and Haser, R. (1998) EMBO J., 17, 5551–5562.Google Scholar
  41. 41.
    Davies, G. J. (1998) Biochem. Soc. Trans., 26, 167–173.Google Scholar
  42. 42.
    Rabinovich, M. L. (1977) Carbohydrase Kinetics (Lysozyme and Cellulolytic Enzymes): Candidate's dissertation [in Russian], School of Chemistry, Moscow State University, Moscow.Google Scholar
  43. 43.
    Klyosov, A. A., and Rabinovich, M. L. (1980) Enzyme Engineering: Future Directions (Wingard, L. V., and Berezin, I. V., eds.) Plenum Press, New York-London, pp. 83–165.Google Scholar
  44. 44.
    Klyosov, A. A., and Rabinovich, M. L. (1989) Tricel 89, Technical University, Vienna, L. 11.Google Scholar
  45. 45.
    Mattinen, M. L., Kontteli, M., and Kerovuo, J. (1997) Protein Sci., 6, 294–303.Google Scholar
  46. 46.
    Jervis, E. J., Haynes, C. A., and Kilburn, D. G. (1997) J. Biol. Chem., 272, 24016–24023.Google Scholar
  47. 47.
    Kraulis, P. J., Clore, G. M., Nigles, M., Jones, T. A., Pettersson, G., Knowles, J. K. C., and Gronenborn, A. M. (1989) Biochemistry, 28, 7241–7257.Google Scholar
  48. 48.
    Hass, G. M., Hermodson, M. A., Ryan, C. A., and Gentry, L. (1982) Biochemistry, 21, 762–766.Google Scholar
  49. 49.
    Mosolov, V. V., and Valueva, T. A. (1993) Plant Proteinase Inhibitors (Kretovich, V. L., ed.) Institute of Biochemistry, Russian Academy of Sciences, Moscow.Google Scholar
  50. 50.
    McFallen, C. A., Svendsen, I., Jonassen, I., and James, M. N. G. (1985) Proc. Natl. Acad. Sci. USA, 82, 7242–7246.Google Scholar
  51. 51.
    Schou, C., Rasmussen, G., Kalloft, M. B., Henrissat, B., and Schulein, M. (1993) Eur. J. Biochem., 217, 947–957.Google Scholar
  52. 52.
    Tomme, P., Warren, R. A. J., Miller, R. C., Jr., Kilburn, D. G., and Gilkes, N. R. (1995) Enzymatic Degradation of Insoluble Carbohydrates (Saddler, J., and Penner, M., eds.) ACS, Washington D. C., USA, pp. 1–12.Google Scholar
  53. 53.
    Kilburn, D. G., Assouline, Z., Din, N., Gilkes, N. R., Ong, E., Tomme, P., and Warren, R. A. J. (1993) Trichoderma reesei Cellulases and Other Hydrolases. Foundation for Biotechnical and Industrial Fermentation (Suominen, P., and Reinikainen, T., eds.) Helsinki, pp. 281–290.Google Scholar
  54. 54.
    Hayashida, S., and Yoshioka, H. (1980) Agric. Biol. Chem., 44, 481–487.Google Scholar
  55. 55.
    Xu, G.-Y., Ong, E., Gilkes, N. R., Kilburn, D. G., Muhandiram, D. R., Harris-Brandts, M., Carver, J. P., Kay, L. E., and Harvey, T. S. (1995) Biochemistry, 34, 6993–7009.Google Scholar
  56. 56.
    Bayer, E. A., Morag, E., Lamed, R., and Shoham, Y. (1998) Curr. Opin. Struct. Biol., 8, 548–557.Google Scholar
  57. 57.
    Abou Hachem, M., Nordberg Karlsson, E., Bartonek-Roxa, E., Raghothama, S., Simpson, P. J., Gilbert, H. J., Williamson, M. P., and Holst, O. (2000) Biochem J., 345, 53–60.Google Scholar
  58. 58.
    Creagh, A. L., Koska, J., Johnson, P. E., Tomme, P., Joshi, M. D., McIntosh, L. P., Kilburn, D. G., and Haynes, C. A. (1998) Biochemistry, 37, 3529–3537.Google Scholar
  59. 59.
    Chapon, V., Czjzek, M., El Hassouni, M., Py, B., Juy, M., and Barras, F. (2001) J. Mol. Biol., 310, 1055–1066.Google Scholar
  60. 60.
    Tomme, P., Boraston, A., McLean, B., Kormos, J., Creagh, A. L., Sturch, K., Gilkes, N. R., Haynes, C. A., Warren, R. A., and Kilburn, D. G. (1998) J. Chromatogr. B. Biomed. Sci. Appl., 715, 283–296.Google Scholar
  61. 61.
    Sunna, A., Gibbs, M. D., and Bergquist, P. L. (2000) Microbiology, 146, 2947–2955.Google Scholar
  62. 62.
    Sunna, A., Gibbs, M. D., and Bergquist, P. L. (2000) Biochem. J., 346, Pt. 3, 583–586.Google Scholar
  63. 63.
    Blake, C. C. F., Koenig, D. F., Mair, G. A., North, A. C. T., Phillips, D. C., and Sarma, V. R. (1965) Nature, 206, 757–763. Google Scholar
  64. 64.
    Rabinovich, M. L., Nguen Van Viet, and Klyosov, A. A. (1982) Biokhimiya, 47, 465–477.Google Scholar
  65. 65.
    Rabinovich, M. L. (1988) Microbiology and Biochemistry of the Decomposition of Plant Raw Materials (Skryabin, G. K., and Golovlev, E. L., eds.) [in Russian], Nauka, Moscow, pp. 70–108.Google Scholar
  66. 66.
    Srisodsuk, M., Reinikainen, T., and Teeri, T. T. (1993) J. Biol. Chem., 268, 20756–20761.Google Scholar
  67. 67.
    Rabinovich, M. L. (1984) Materials of Soviet-Finland Seminar on Bioconversion of Plant Raw Materials by Microorganisms, Institute of Biochemistry and Physiology of Microorganisms, Pushchino, pp. 31–48.Google Scholar
  68. 68.
    Rabinovich, M. L., Chernoglazov, V. M., Klyosov, A. A., Nguen Van Viet, and Berezin, I. V. (1981) Doklady AN SSSR. Ser. Biokhim., 260, 1481–1486.Google Scholar
  69. 69.
    Klyosov, A. A., and Rabinovich, M. L. (1980) Materials II Int. Symp. on Bioconversion and Biochem. Engineering, Scylark Printers, New Dehli, pp. 53–56.Google Scholar
  70. 70.
    Henriksson, G., Nutt, A., Henriksson, H., and Pettersson, L. G. (1999) Eur. J. Biochem., 259, 88–95.Google Scholar
  71. 71.
    Rabinovich, M. L., Chernoglazov, V. M., and Klyosov, A. A. (1983) Biokhimiya, 48, 369–377.Google Scholar
  72. 72.
    Rabinovich, M. L., Melnick, M. S., Badalov, A. B., Klyosov, A. A., and Berezin, I. V. (1985) Doklady AN SSSR. Ser. Biokhim., 282, 1013–1017.Google Scholar
  73. 73.
    Knowles, J., Teerei, T. T., Lehtovaara, P., Penttila, M., and Saloheimo, M. (1988) Biochemistry and Genetics of Cellulose Degradation (Aubert, J.-P., and Beguin, B., eds.) Academic Press, Paris, pp. 153–169.Google Scholar
  74. 74.
    Rabinovich, M. L., Klyosov, A. A., and Berezin, I. V. (1984) Doklady AN SSSR. Ser. Biokhim., 274, 758–763.Google Scholar
  75. 75.
    Rabinovich, M. L., Novikova, T. V., Klyosov, A. A., and Berezin, I. V. (1985) Bioorg. Khim., 11, 1343–1347.Google Scholar
  76. 76.
    Rabinovich, M. L., Klyosov, A. A., and Melnick, M. S. (1986) Analyt. Biochem., 156, 489–494.Google Scholar
  77. 77.
    Linder, M., and Teerei, T. T. (1996) Proc. Natl. Acad. Sci. USA, 93, 12251–12255.Google Scholar
  78. 78.
    Rabinovich, M. L. (1984) Abst. XVI FEBS Conf., Moscow, p. 393.Google Scholar
  79. 79.
    Rabinovich, M. L., Nguen Van Viet, and Klyosov, A. A. (1986) Prikl. Biokhim. Mikrobiol., 22, 70–79.Google Scholar
  80. 80.
    Barr, B. K., Hsieh, Y.-L., Ganem, B., and Wilson, D. B. (1996) Biochemistry, 35, 586–592.Google Scholar
  81. 81.
    Reverbel-Leroy, C., Parsiegla, G., and Moreau, V. (1998) Acta Crystallogr. D. Biol. Crystallogr., 54, Pt. 1, 114–118.Google Scholar
  82. 82.
    Herner, M. L., Melnick, M. S., and Rabinovich, M. L. (1999) Biochemistry (Moscow), 64, 1012–1020.Google Scholar
  83. 83.
    Melnick, M. S., Rabinovich, M. L., and Voznyi, Ya. V. (1991) Biokhimiya, 56, 1787–1797.Google Scholar
  84. 84.
    Herner, M. L., Melnick, M. S., Leontyeva, G. V., Romenskaya, I. G., and Rabinovich, M. L. (2000) Prikl. Biokhim. Mikrobiol., 36, 5–7.Google Scholar
  85. 85.
    Gusakov, A. V., Sinitsyn, A. P., and Klyosov, A. A. (1986) Prikl. Biokhim. Mikrobiol., 22, 59–69.Google Scholar
  86. 86.
    Converse, A. O., Ooshima, H., and Burns, D. S. (1990) Appl. Biochem. Biotechnol., 24/25, 67–73.Google Scholar
  87. 87.
    Obraztsova, I. N., Fedosenko, M. A., and Rabinovich, M. L. (1993) Prikl. Biokhim. Mikrobiol., 29, 684–689.Google Scholar
  88. 88.
    Henriksson, G., Johansson, G., and Pettersson, G. (2000) J. Biotechnol., 78, 93–113.Google Scholar
  89. 89.
    Yuldashev, B. T., Rakhimov, M. M., and Rabinovich, M. L. (1993) Prikl. Biokhim. Mikrobiol., 29, 58–68.Google Scholar

Copyright information

© MAIK “Nauka/Interperiodica” 2002

Authors and Affiliations

  • M. L. Rabinovich
    • 1
    Email author
  • M. S. Melnick
    • 1
  • A. V. Bolobova
    • 1
  1. 1.Bach Institute of BiochemistryRussian Academy of SciencesMoscowRussia

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