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David Zechel:  Publications

Dr. Zechel's Research Page

32. Michael Suits, Yanping Zhu, Edward Taylor, Julia Walton, David Zechel, Harry Gilbert, and Gideon Davies “Structure and kinetic investigation of Streptococcus pyogenes family GH38 a-mannosidase.” PLOS One (2009): 5:e9006.


31. Podzelinska K, Latimer R, Bhattacharya A, Vining LC, Zechel DL, Jia Z: "The structure of CmlS, a flavin-dependent halogenase involved in the biosynthesis of chloramphenicol". J. Mol. Biol. (2010): 397:316-331.


30. Hove-Jensen B, Rosenkrantz TJ, Zechel DL, Willemoës M: "Accumulation of intermediates of the carbon-phosphorus lyase pathway for phosphonate degradation in phn mutants of E. coli. J. Bacteriol". (2010), 192:370-4.


29. He SM, Luo Y, Hove-Jensen B, Zechel DL: "A fluorescent substrate for carbon-phosphorus lyase: towards the pathway for organophosphonate metabolism in bacteria". Bioorg. Med. Chem. Lett. (2009), 19:5954-7.


28. Latimer R, Podzelinska K, Soares A, Bhattacharya A, Vining LC, Jia Z, Zechel DL: "Expression, purification and preliminary diffraction studies of CmlS". Acta. Crystallogr. Sect. F Struct. Biol. Cryst. Commun. (2009), 65:260-263.


27. Podzelinska K, He SM, Wathier M, Yakunin A, Proudfoot M, Hove-Jensen B, Zechel DL, Jia Z: "Structure of PhnP, a phosphodiesterase of the carbon-phosphorus lyase pathway for phosphonate degradation". J. Biol. Chem. (2009), 284:17216-17226.


26. Tailford LE, Ducros VM, Flint JE, Roberts SM, Morland C, Zechel DL, Smith N, Bjornvad ME, Borchert TV, Wilson KS, Davies GJ, Gilbert HJ: "Understanding how diverse b-mannanases recognize heterogeneous substrates". Biochemistry (2009), 48:7009-7018.


25. Offen WA, Zechel DL, Withers SG, Gilbert HJ, Davies GJ: "Structure of the Michaelis complex of b-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis". Chem. Commun. (Camb) (2009): 2484-2486.


24. R. Latimer, K. Podzelinska, A. Soars, A. Bhattacharya, L. Vining, Z. Jia, D.L. Zechel "Expression, purification and preliminary diffraction studies of CmlS, a flavin dependant halogenase" Acta Crystallogr Sect F Struct Biol Cryst Commun (2009), 65, 260-3.


23. K. Podzelinska, S.-M. He, M. Wathier, M. Proudfoot, A. Yakunin, B. Hove-Jensen, D.L. Zechel,      Z. Jia, "Structure of PhnP: A Phosphodiesterase of the Carbon-Phosphorous Lyase Pathway for Phosphonate Degredation" J Biol Chem (2009), in press.


22.  M.A. Adams, Y. Luo, B. Hove-Jensen, S.M. He, L.M. van Staalduinen, D.L. Zechel, Z. Jia, "Crystal Structure of PhnH: An Essential Component of Carbon-Phosphorus Lyase in Escherichia coli" J Bacteriol (2008), 190, 1072-83.


21.  K. Podzelinska, S.M. He, A. Soares, D.L. Zechel, B. Hove-Jensen, Z. Jia, "Expression, Purification and Preliminary Diffraction Studies of PhnP" Acta Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. (2008), 64, 554-7.


20.  L.M. van Staalduinen, A. Bhattacharya, K. Groom, D.L. Zachel, Z. Jia, "Expression, Purification and Preliminary X-Ray Diffraction Studies of RebC" Acta Crystallogr Sect F Struct Biol Cryst Commun (2007), 63, 980-982.


19.  T.M. Gloster, P. Meloncelli, R.V. Stick, D.L. Zechel, A. Vasella, G.J. Davies "Glycosidase Inhibition: an Assessment of the Binding of 18 Putative Transition-State Mimics" J Am Chem Cos (2007), 129, 2345-2354.


18.  Y. Luo, D.L. Zechel, "A Concise Synthesis of a α-D-ribofuranosyl alkylphosphonates - Putative Substrate Intermediates for the Carbon-Phosphorous Lyase System." Can J. Chem. (2006), 84, 743-747.


17.  T. Matsuura, A. Ernst, D.L. Zechel, A. Plückthun, "Combinatorial Approaches to Novel Proteins"  Chem. Biol., 2003, in press.


16.  D.L. Zechel, A.B. Boraston, T. Gloster, K. Boraston, J.M. Macdonald, D.M.G. Tilbrook, R.V. Stick , G.J. Davies,  “Azasugar Glycosidase Inhibitors: Structural and Thermodynamic Dissection of the Binding of Isofagomine and 1-deoxynojirimycin to Two ß-glucosidases.”  J. Am. Chem. Soc. 2003, in press


15.  A. Varrot, C.A. Tarling, J. Macdonald, R.V. Stick, D.L. Zechel, S.G. Withers, G.J. Davies,  “Direct Observation of the Protonation of an Imino-Sugar Glycosidase Inhibitor Upon Binding.”  J. Am. Chem. Soc. 2003, 125, 7496-7497.


14.  V.M-.A. Ducros, C.A. Tarling, D.L. Zechel, A.M. Brzozowski, T.P. Frandsen, I. von Ossowski, M. Schülein, S.G. Withers, G.J. Davies,  “Anatomy of Glycosynthesis:  Structure and Kinetics of the Humicola Insolens Cel7B E197A and E197S Glycosynthase Mutants.”  Chem. Biol. 2003, 10, 1-10.


13.  G.J. Davies, V.M-.A. Ducros, A. Varrot, D.L. Zechel,  “Mapping the Conformational Itinerary of ß-glycosidases by X-Ray Crystallography.” Biochem. Soc. Trans. 2003, 31, 523-527.


12.  D.L. Zechel, S.P. Reid, D. Stoll, O. Nashiru, R.A.J. Warren, S.G. Withers,  “Mechanism, Mutagenesis and Chemical Rescue of a ß-Mannosidase from Cellulomonas fimi.”  Biochemistry 2003, 42, 7195-7204.


11.  V.M.-A. Ducros, D.L. Zechel, G.N. Murshudov, H.J. Gilbert, L. Szabó, D. Stoll, S.G. Withers, G.J. Davies,  “Substrate Distortion by a ß-mannanase:  Snapshots of the Michaelis and Covalent-intermediate Complexes Suggest a B2,5 Conformation for the Transition State.”  Angew. Chem. Int. Ed. 2002, 41, 2824-2827.


10.  D.L. Zechel, S.G. Withers,  “Dissection of Nucleophilic and Acid-Base Catalysis in Glycosidases.”  Curr. Opin. Chem. Biol. 2001, 5, 643-649.


9.  D.L. Zechel, S.P. Reid, O. Nashiru, C. Mayer, D. Stoll, D.L. Jakeman, R.A.J. Warren, S.G. Withers,  “Enzymatic Synthesis of Carbon-fluorine Bonds.”  J. Am. Chem. Soc. 2001, 123, 4350-4351.


8.  O. Nashiru, D.L. Zechel, D. Stoll, T. Mohammedzadeh, R.A.J. Warren, S.G. Withers,  “b-Mannosynthase:  synthesis of ß-mannosides with a mutant ß-mannosidase.”  Angew. Chem. Int. Ed. 2001, 40, 417-420.


7.  C. Mayer, D.L. Zechel, S.P. Reid, R.A.J. Warren, S.G. Withers,  “The E358S Mutant of Agrobacterium sp. ß-glucosidase is a Greatly Improved Glycosynthase.”  FEBS Lett. 2000, 466, 40-44.


6.  D.L. Zechel and S.G. Withers,  “Glycosidase Mechanisms:  Anatomy of a finely tuned catalyst.”  Acc. Chem. Res. 2000, 33, 11-18.


5.  D.L. Zechel and S.G. Withers, "Glycosyl Transferase Mechanisms" In Comprehensive Natural Products Chemistry, C.D. Poulter, Ed., Elsevier: New York, 1999, vol. 5, pp 279-314.


4.  D.L. Zechel, L. Konermann, S.G. Withers,  D.J. Douglas,  “Pre-steady State Kinetic Analysis of an Enzymatic Reaction Monitored by Time-resolved Electrospray Ionization Mass Spectrometry.”  Biochemistry 1998, 37, 7664-7669.


3.  D.L. Zechel, S. He, C. Dupont, S.G. Withers,  “Identification of Glu-120 as the Catalytic Nucleophile in Streptomyces lividans endoglucanase CelB.”  Biochem. J. 1998, 336, 139-145.


2.  D.L. Zechel, K.C. Hultzsch, R. Rulkens, D. Balaishis, Y. Ni, J.K. Pudelski, A.J. Lough, I. Manners, D.A. Foucher,  “Thermal and Transition-metal-catalyzed Ring-Opening Polymerization (ROP) of [1]Silaferrocenophanes with Chlorine Substituents at Silicon:  A Route to Tunable Poly(ferrocenylsilanes).”  Organometallics 1996, 15, 1972-1978.


1.  D.L. Zechel, D.A. Foucher, J.K. Pudelski, G.P.A. Yap, A.L. Rheingold, I. Manners,  “Synthesis, Structural Characterization, Electrochemical Properties and Polymerization Behaviour of the First Silicon-bridged [1.1]ferrocenophane [{Fe(h-C5H4)2SiMe2}2].”  J. Chem. Soc., Dalton Trans. 1995, 1893-1899.


14.  Enzymatic Halogenation in Natural Product Biosynthesis”  Dept. od Chemistry and Biochemistry, Trent University, March 13th 2009.


13.  Analysis of PhnP from the carbon-phosphorous lyase pathway”  Canadian Society for Chemistry national meeting, Altered Proteins Symposium, Edmonton, May 2008.


12.  Functional and structural analysis of the carbon-phosphorous lyase pathway”  4th Annual McGill Biophysical Chemistry Symposium, McGill University, May 2008.


11.  Towards the catalytic mechanism of carbon-phosphorous lyase”  Canadian Society for Chemistry national meeting, Winnipeg, November 2006.


10.  Structural and functional characterization of an enzyme essential for carbon phosphorous bond cleavage activity in bacteria”  34th Ontario-Quebec Physical Prganic Mini-Symposium, Montreal, November 2006.


9.  Teaching proteins new tricks: from SH2 domains to carbon-phosphorous lyase.”  Canadian Society for Chemistry national meeting, Advances in Protein Engineering symposium, Halifax, May 2006.


8.  Towards the mechanism of carbon-phosphorous lyase.”  Departments of Chemistry and Biochemistry, York University, Toronto, April 2006.


7.  In vitro selection technologies for probing protein function”  Protein Engineering Centres of Excellence (PENCE) seminar series, Department of Biochemistry, University of Toronto, February 2005.


6.  In vitro selection technologies for probing protein function”  Deptartment of Biolchemistry, Queen's University, Kingston, Ontario, November 2004.


5.  “Catalytic Promiscuity of Glycosynthases.”  Dept. of Biological and Nutritional Sciences, The University of Newcastle upon Tyne, Newcastle upon Tyne, United Kingdom, November 2001.


4.   “Catalytic Promiscuity of Glycosynthases.”  Biomolecular Sciences Seminar Programme, Centre of Biomolecular Sciences, University of St. Andrews, St. Andrews, United Kindom, October 2001.


 3.  “Catalytic Promiscuity of Glycosynthases.”  Biochemisches Institut, Universität Zürich, Zürich, Switzerland, June 2001


2.  “Catalytic Mechanisms of the Glycosyl Hydrolases.”  Gordon Research Conference on ‘Cellulases and Cellulosomes’, Proctor Academy, Andover, New Hampshire, July 1999.


1.  “Glycosynthases:  Advances and Future Prospects.”  Protein Engineering Network of Centres of Excellence annual meeting, Toronto, Ontario, May 1997.