Peter Moody

Peter Moody studied biochemistry at the University of York, where he worked on the structure of barnase with Guy & Eleanor Dodson and he was awarded the Ph.D. degree in biophysics from Imperial College in 1984, where he studied the structure and function of glyceraldehyde-3-phosphate dehydrogenase with Alan Wonacott in David Blow’s group. His postdoctoral work has been at Harvard with W.N. Lipscomp Jnr., at Imperial with Andrew Leslie and in York with Guy Dodson. Amongst the structures he has solved have been penicillin acylase (for which he proposed the “N-terminal nucleophile” mechanism), the suicidal DNA repair protein (O6alkylguanine-DNA alkyltransferase), the flavoenzymes PETN reductase & morphinone reductase & serine acetyl transferase. His current research interests include the structure and mechanisms of heme redox enzymes and of glycolytic enzymes from pathogens. He took his current post at the University of Leicester in 1995, where he sat up the protein crystallography laboratory. He has been a member of the Council of the British Crystallographic Association and is currently the Synchrotron Radiation User Group representative of the UK protein crystallography community. To date he has over 50 papers that have been cited over 2000 times.

Biography Updated on 20 November 2007

Personal Home Page

http://www.le.ac.uk/biochem/staff/pcem1/pcem1.html

Articles in Scholarly Journals [Incomplete List]

  1. The Redox Properties of Ascorbate Peroxidase
    Biochemistry, vol. 46, no. 27, pp. 8017–8023, 2007
  2. Filling a Hole in Cytochrome P450 BM3 Improves Substrate Binding and Catalytic Efficiency
    Journal of Molecular Biology, vol. 373, no. 3, pp. 633–651, 2007
  3. Biochemistry, vol. 45, no. 25, pp. 7808–7817, 2006
  4. Conformational Mobility in the Active Site of a Heme Peroxidase
    Journal of Biological Chemistry, vol. 281, no. 34, pp. 24512–24520, 2006
  5. Biochemistry, vol. 43, no. 27, pp. 8644–8651, 2004
  6. Enzyme-catalyzed Mechanism of Isoniazid Activation in Class I and Class III Peroxidases
    Journal of Biological Chemistry, vol. 279, no. 37, pp. 39000–39009, 2004
  7. The Structure and Mechanism of Serine Acetyltransferase from Escherichia coli
    Journal of Biological Chemistry, vol. 279, no. 39, pp. 40729–40736, 2004
  8. Atomic Resolution Structures and Solution Behavior of Enzyme-Substrate Complexes of Enterobacter cloacae PB2 Pentaerythritol Tetranitrate Reductase: MULTIPLE CONFORMATIONAL STATES AND IMPLICATIONS FOR THE MECHANISM OF NITROAROMATIC EXPLOSIVE DEGRADATION
    Journal of Biological Chemistry, vol. 279, no. 29, pp. 30563–30572, 2004
  9. Crystal structure of the ascorbate peroxidase–ascorbate complex
    Nature Structural Biology, vol. 10, no. 4, Article ID nsb913, 4 pages, 2003
  10. A new framework for understanding substrate binding and functional diversity in haem peroxidases
    Dalton Transactions, no. 22, p. 4208, 2003
  11. Crystal Structure of Bacterial Morphinone Reductase and Properties of the C191A Mutant Enzyme
    Journal of Biological Chemistry, vol. 277, no. 34, pp. 30976–30983, 2002
  12. Kinetic and Structural Basis of Reactivity of Pentaerythritol Tetranitrate Reductase with NADPH, 2-Cyclohexenone, Nitroesters, and Nitroaromatic Explosives
    Journal of Biological Chemistry, vol. 277, no. 24, pp. 21906–21912, 2002
  13. Effects of environment on flavin reactivity in morphinone reductase: analysis of enzymes displaying differential charge near the N-1 atom and C-2 carbonyl region of the active-site flavin
    Biochemical Journal, vol. 359, no. 2, p. 315, 2001
  14. Crystal structure of pentaerythritol tetranitrate reductase: “flipped” binding geometries for steroid substrates in different redox states of the enzyme
    Journal of Molecular Biology, vol. 310, no. 2, pp. 433–447, 2001
  15. Serine Acetyltransferase from Escherichia coli Is a Dimer of Trimers
    Journal of Biological Chemistry, vol. 275, no. 1, pp. 461–466, 2000
  16. DNA-binding mechanism of the Escherichia coli Ada O6-alkylguanine-DNA alkyltransferase
    Nucleic Acids Research, vol. 28, no. 19, pp. 3710–3718, 2000
  17. Crystal structure of the human O6-alkylguanine-DNA alkyltransferase
    Nucleic Acids Research, vol. 28, no. 2, pp. 393–401, 2000
  18. Crystal structure of Trematomus newnesi haemoglobin re-opens the root effect question
    Journal of Molecular Biology, vol. 287, no. 5, pp. 897–906, 1999
  19. Analysis and characterization of data from twinned crystals
    Acta Crystallographica Section D Biological Crystallography, vol. 55, no. 10, pp. 1750–1758, 1999
  20. The structure of the exo-ß-(1,3)-glucanase from Candida albicans in native and bound forms: relationship between a pocket and groove in family 5 glycosyl hydrolases
    Journal of Molecular Biology, vol. 294, no. 3, pp. 771–783, 1999
  21. Biochemistry, vol. 37, no. 20, pp. 7598–7607, 1998
  22. Ligand-induced conformational change in penicillin acylase
    Journal of Molecular Biology, vol. 284, no. 2, pp. 463–475, 1998
  23. Crystallization and preliminary diffraction studies of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2
    Acta Crystallographica Section D Biological Crystallography, vol. 54, no. 4, pp. 675–677, 1998
  24. The potential role of glycine-160 of human O6-alkylguanine-DNA alkyltransferase in reaction with O6-benzylguanine as determined by site-directed mutagenesis and molecular modelling comparisons
    Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol. 1342, no. 1, pp. 90–102, 1997
  25. Crystallization and preliminary diffraction studies of morphinone reductase, a flavoprotein involved in the degradation of morphine alkaloids
    Acta Crystallographica Section D Biological Crystallography, vol. 53, no. 5, pp. 619–621, 1997
  26. A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm
    Structure, vol. 5, no. 5, pp. 623–633, 1997
  27. Penicillin acylase has a single-amino-acid catalytic centre
    Nature, vol. 373, no. 6511, Article ID 373264a0, 4 pages, 1995
  28. Biochemistry, vol. 34, no. 47, pp. 15553–15563, 1995
  29. A protein catalytic framework with an N-terminal nucleophile is capable of self-activation
    Nature, vol. 378, no. 6555, Article ID 378416a0, 3 pages, 1995
  30. The crystal structure of a major secreted aspartic proteinase from Candida albicans in complexes with two inhibitors
    Structure, vol. 3, no. 11, pp. 1261–1271, 1995
  31. Crystal structure of an extracellular fragment of the rat CD4 receptor containing domains 3 and 4
    Structure, vol. 2, no. 6, pp. 469–481, 1994
  32. Crystallization of Inhibited Aspartic Proteinase from Candida albicans
    Journal of Molecular Biology, vol. 234, no. 4, pp. 1266–1269, 1993
  33. Crystallization of O6-methylguanine-DNA methyltransferase from Escherichia coli
    Journal of Molecular Biology, vol. 200, no. 4, pp. 751–752, 1988
  34. Structure of Chloramphenicol Acetyltransferase at 1.75- angstrom Resolution
    Proceedings of the National Academy of Sciences, vol. 85, no. 12, pp. 4133–4137, 1988
  35. Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from at 1.8 p resolution
    Journal of Molecular Biology, vol. 193, no. 1, pp. 171–187, 1987