Chitinases

  • Natural Substrate Assay for Chitinases Using High Performance Liquid Chromatography: A Comparison with Existing Assays; I.M. Krokeide, B. Synstad, S. Gåseidnes, S. J. Horn, V.G.H. Eijsink, M. Sørlie. Anal. Biochem., in press.
  • Precise and Continuous Enzyme Assay for Chitinase Catalyzed Hydrolysis of Tetra-N-acetylchitotetraose Using Isothermal Titration Calorimetry. I.-M. Krokeide, V.G.H. Eijsink, M. Sørlie. Thermochimica Acta, in press.
  • Mucolytic activity of bacterial and human chitinases. N. N. Sanders, V.G.H. Eijsink, P.S. van den Pangaart, R.J. van Neerven, P.J. Simons, S.C. De Smedt, J. Demeester, Biochim. Biophys. Acta, in press.
  • Enzymatic degradation of recalcitrant polysaccharides: costs and benefits of processivity S.J. Horn, P. Sikorski, J.B. Cederkvist, G. Vaaje-Kolstad, M. Sørlie, B. Synstad, G. Vriend, K.M. Vårum, V.G.H. Eijsink; Proc. Natl. Acad. Sci. USA 103(2006) 18089-18094.
  • Serratia marcescens chitinases with “tunnel-shaped” substrate-binding grooves show endo-activity and different degrees of processivity during enzymatic hydrolysis of chitosan; P. Sikorski, A. Sørbotten, S. J. Horn, V. G. H. Eijsink, K. M. Vårum; Biochemistry, 45(2006) 9566-9574.
  • Crystal structure and enzymatic properties of a bacterial family 19 chitinase reveal differences with plant enzymes; I.A. Hoell, B. Dalhus, E.B. Heggset, S.I. Aspmo, V.G.H. Eijsink; FEBS J. 273 (2006) 4889-4900.
  • Molecular cloning, characterization, and real-time expression studies of a novel endochitinase gene (ech30) from the mycoparasite Trichoderma atroviride strain P1. S.S. Klemsdal, J.L. Clarke, I.A. Hoell, V.G.H. Eijsink, M.B. Brurberg; FEMS Microbiol. Lett. 256(2006) 282-289.
  • Synthesis and evaluation of a 99mTc-HYNIC-labeled chitin-binding protein as potential specific radioligand for the in vivo detection of fungal infections in mice. R. Siaens, V.G.H. Eijsink, G. Vaaje-Kolstad, K. Vandenbulcke, B. Cornelissen, R. Dierckx, G. Slegers, Quart. J. Nucl. Medic. Mol. Imaging 50 (2006)155-166.
  • Identification of non-covalent glycosidase chitooligosaccharide complexes by (+) nanoelectrospray quadrupole time-of-flight mass spectrometry. F.C. Cederkvist, A. Zamfir, V.G.H. Eijsink, M. Sørlie, J. Peter-Katalinic, M.G. Peter; Ang Chemie Int Ed. 45(2006) 2429-2434
  • Endo/exo mechanism and processivity of family 18 chitinases produced by Serratia marcescens. S.J. Horn, A. Sørbotten, B. Synstad, P. Sikorski, M. Sørlie, K.M. Vårum, V.G.H. Eijsink; FEBS J. 273 (2006) 491-503.
  • Comparative studies of chitinases A, B, and C from Serratia marcescens. S.J. Horn, M. Sørlie, A.L. Norberg, B. Synstad, G. Vaaje-Kolstad, K.M. Vårum, V.G.H. Eijsink; Biocatalysis and Biotransformation, 24 (2006) 39-53.
  • The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation; Vaaje-Kolstad, G., S.J. Horn, D.M.F. van Aalten, B. Synstad, and V.G.H. Eijsink; Journal of Biological Chemistry, 2005. 280(31): p. 28492-28497. pdf
  • Directed Evolution of Enzyme Stability; Eijsink, V.G.H., A. Bjork, S. Gaseidnes, R. Sirevag, B. Synstad, B. van den Burg, and G. Vriend; Biomolecular Engineering (2005) 22(1-3): p. 21-30. pdf
  • Overexpression and characterisation of a new chitinase from Trichoderma atroviride strain P1; I. A. Hoell, S. S. Klemsdal, G. Vaaje-Kolstad, S. J. Horn, V.G.H. Eijsink, Biochim. Biophys. Acta 1748 (2005) 180-190. pdf
  • Development and application of a model for chitosan hydrolysis by a family 18 chitinase; P. Sikorski, B.T. Stokke, A. Sørbotten, K.M. Vårum, S.J. Horn, V.G.H. Eijsink; Biopolymers 77 (2005) 273-285. pdf
  • Crystal structure and binding properties of the chitin-binding protein from Serratia marcescens; G. Vaaje-Kolstad, D.R. Houston, V.G.H. Eijsink, D.M.F. van Aalten; J. Biol. Chem. 280 (2005) 11313-11319. pdf
  • Degradation of chitosans with Chitinase B from Serratia marcescens; production of chito-oligosaccharides and insight in enzyme processivity; A. Sørbotten, S.J. Horn, V.G.H. Eijsink, K.M. Vårum; FEBS J. 272 (2005) 1523-1534. pdf
  • Structure-based optimization of a family 18 chitinase cyclic dipeptide inhibitor; D.R. Houston, B. Synstad, V.G.H. Eijsink, I. Eggleston, D.M.F. van Aalten; J. Med. Chem.. 47 (2004) 5713-5720. pdf
  • Rational engineering of enzyme stability; V.G.H. Eijsink, S. Gåseidnes, B. Synstad, A. Bjørk, R. Sirevåg, B. Van den Burg, G. Vriend, G.; J. Biotechnol. 113 (2004) 105-20. pdf
  • 123I-Labeled Chitinase as Specific Radioligand for In Vivo Detection of Fungal Infections in Mice; R. Siaens, V.G.H. Eijsink, R. Dierckx, G. Slegers; J. of Nuclear Medicine 45 (2004) 1209-1216. pdf
  • A reliable reducing end assay for chito-oligosaccharides; S.J. Horn, V.G.H. Eijsink; Carbohydrate Polymers 56 (2004) 35-39. pdf
  • Structure of the D142N mutant of the family 18 chitinase ChiB from Serratia marcescens and its complex with allosamidin; G. Vaaje-Kolstad D.R. Houston, F.V. Rao, M.G. Peter, B. Synstad, D.M.F. van Aalten, V.G.H. Eijsink; Biochim. Biophys. Acta 1696 (2004) 103-111. pdf
  • Interactions of a family 18 chitinase with HM508, a designed inhibitor; G. Vaaje-Kolstad, A. Vasella, M.G. Peter, C. Netter, D.R. Houston, B. Westereng, B. Synstad, V.G.H. Eijsink, D.M.F. van Aalten; J. Biol. Chem. 279 (2004) 3612-3619. pdf
  • Mutational and computational analysis of the role of conserved residues in the active site of a family 18 chitinase; B. Synstad, S. Gåseidnes, D.M.F. van Aalten, G. Vriend, J.E.Nielsen, V.G.H. Eijsink; Eur. J. Biochem. 271 (2004) 253-262.
  • Book chapter: Details in the reaction mechanism of chitinases; V.G.H. Eijsink, G. Kolstad, S. Gåseidnes, B. Synstad, M.G. Peter, J.E. Nielsen, D. Komander, D. Houston, D.M.F. van Aalten; In: Enzyme functionality: design, engineering and screening (A. Svendsen, ed.); Marcel Dekker Inc., New York, pp 229-246 (2003)
  • Book chapter: Structure and function of chitinolytic enzymes; V.G.H. Eijsink, B. Synstad, G. Kolstad, S. Gåseidnes, D. Komander, M.G. Peter, D.M.F. Van Aalten; Adv. Chitin Science VI (Vårum, K.M., Domard, A. & Smidsrød, O., eds.), NTNU Trondheim, pp. 71-78 (2003).
  • Rational engineering of the stability and the catalytic performance of enzymes; S. Gåseidnes, B. Synstad, J.E. Nielsen, V.G.H. Eijsink; J. Molecular Catalysis, B: Enzymatic 21 (2003) 3-8.
  • Electrostatic interactions across the dimer-dimer interface contribute to the pH-dependent stability of a tetrameric malate dehydrogenase; Bjork, A., D. Mantzilas, R. Sirevag, and V.G.H. Eijsink, . Febs Letters; (2003) 553(3): p. 423-426. pdf
  • Stabilization of a chitinase from Serratia marcescens by Gly -> Ala and Xxx -> Pro mutations; S. Gåseidnes, B. Synstad, X. Jia, H. Kjellesvik, G. Vriend, V.G.H. Eijsink; Protein Engineering 16 (2003) 841-846. pdf
  • The cyclic dipeptide CI-4 [cyclo-(L-Arg-D-Pro)] inhibits family 18 chitinases by structural mimicry of a reaction intermediate. Douglas R. Houston, Ian Eggleston, Bjørnar Synstad, Vincent G. H Eijsink and Daan M. F. van Aalten. Biochem. J. 368 (2002) 23-27. pdf
  • High-resolution structures of a chitinase complexed with natural product cyclopentapeptide inhibitors: Mimicry of carbohydrate substrate. Douglas R. Houston, Kazuro Shiomi, Noriko Arai, Satoshi mura, Martin G. Peter, Andreas Turberg, Bjørnar Synstad, Vincent G. H. Eijsink, and Daan M. F. van Aalten. Proc. Natl. Acad. Sci. USA. 99 (2002) 9127-9132. pdf
  • Psammaplin A, a chitinase inhibitor isolated from the fijian marine sponge Aplysinella rhax. J. N. Tabudravu, V. G. H. Eijsink, G. W. Gooday, M. Jaspars, D. Komander, M. Legg, B. Synstad and D. M. F. van Aalten, Bioorganic & Medicinal Chemistry. 10 (2002) 1123-1128. pdf
  • Structural insights into the catalytic mechanism of a family 18 exochitinase; D. M. F. van Aalten, D. Komander, B. Synstad, S. Gåseidnes,M. G. Peter, and V. G. H. Eijsink (2001). Proceedings of the National Academy of Sciences of the United States of America. 16, 8979-8984. pdf
  • Crystal structure of the D140N mutant of chitinase B from Serratia marcescens at 1.45 Å resolution; G. Kolstad, B. Synstad, V.G.H. Eijsink, D.M.F. Van Aalten, D58 (2002) 377-379 pdf
  • Synthesis of pseudosugar analogues of chitotriose; Thiele, A. Rottmann, A. Germer, E. Kleinpeter, K.-D. Spindler, B. Synstad, V. G. H. Eijsink and M. G. Petera*;Journal of Carbohydrate Chemistry, (2002) 21(6): p. 471-489 pdf
  • Chitinases from Serratia marcescens; M.B. Brurberg, B. Synstad, S. Klemsdal, D.M.F. Van Aalten, L. Sundheim, V.G.H. Eijsink; Recent Research Developments in Microbiology 5 (2001)187-204
  • Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9 Å resolution; D.M.F. van Aalten, B. Synstad, M.B. Brurberg, E. Hough, B. Riise, V.G.H. Eijsink, R.K. Wierenga; Proc. Natl. Acad. Sci. USA 97 (2000) 5842-5847. pdf
  • On the contribution of conserved acidic residues to catalytic activity of chitinase B from Serratia marcescens; B. Synstad, S. Gåseidnes, G. Vriend, J.-E. Nielsen, V.G.H. Eijsink; in: Advances in Chitin Science (M.G. Peter, R.A.A. Muzzarelli, A. Domard, eds.), Vol. 4, 524-529 (2000).
  • Libraries of chito-oligosaccharides of mixed acetylation patterns and their interactions with chitinases; M.C. Letzel, B. Synstad, V.G.H. Eijsink, J. Peter-Katalinic, M.G. Peter; in: Advances in Chitin Science (M.G. Peter, R.A.A. Muzzarelli, A. Domard, eds.), Vol. 4, 545-552 (2000).
  • Approaches towards the design of new chitinase inhibitors; A. Rottman, B. Synstad, G. Thiele, D. Schanzenbach, V.G.H. Eijsink, M.G. Peter; in: Advances in Chitin Science (M.G. Peter, R.A.A. Muzzarelli, A. Domard, eds.), Vol. 4, 553-557 (2000).
  • Synthesis of N-acetylglucosaminyl and diacetylchitobiosyl amides of heterocyclic carboxylic acids as potential chitinase inhibitors; A. Rottman, B. Synstad, V.G.H. Eijsink, M.G. Peter; Eur. J. Organic Chemistry 1999, 2293-2297. pdf
  • The chitinolytic system of Serratia marcescens; M.B. Brurberg, I.F. Nes, V.G.H. Eijsink; In: Chitin Enzymology (R.A.A. Muzarelli, ed.), Eur. chitin society, Ancona, Italy, 1996, pp. 171-180.
  • Comparative studies of chitinases A and B from Serratia marcescens; M.B. Brurberg, I.F. Nes, V.G.H. Eijsink; Microbiology 142 (1996) 1581-1589.
  • Chitinase B from Serratia marcescens BJL200 is exported to the periplasm without processing; M.B. Brurberg, V.G.H. Eijsink, A.J. Haandrikman, G. Venema, I.F. Nes; Microbiology 141 (1995) 123-131.