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Publications

  1. Sychantha D, Jones CS, Little DJ, Moynihan PJ, Robinson H, Galley NF, Roper DI, Dowson CG, Howell PL, Clarke AJ (2017) In vitro characterization of the antivirulence target of Gram-positive pathogens, peptidoglycan O-acetyltransferase A (OatA) PLOS Pathogens. 13 (10) e1006667
  2. Tran AT, Watson EE, Pujari V, Conroy T, Dowman LJ, Giltrap AM, Pang A, Wong WR, Linington RG, Mahapatra S, Saunders J, Charman SA, West NP, Bugg TD, Tod J, Dowson CG, Roper DI, Crick DC, Britton WJ, Payne RJ. (2017) Sansanmycin natural product analogues as potent and selective anti-mycobacterials that inhibit lipid I biosynthesis. Nature Communications 8: 14414 doi: 10.1038/ncomms14414.
  3. Vajs J, Proud C, Brozovic A, Gazvoda A, Lloyd A, Roper DI, Osmak M, Košmrlj J, Dowson CG. (2017) Diaryltriazenes as antibacterial agents against methicillin resistant Staphylococcus aureus (MRSA) and Mycobacterium smegmatis. Eur J Med Chem. 127 223-234.
  4. Calvez P, Breukink E, Roper DI, Dib M, Contreras-Martel C, Zapun A, (2017) Substitutions in PBP2b from β-lactam resistant Streptococcus pneumoniae have different effects on enzymatic activity and drug reactivity. J Biol Chem. 292(7) 2854-2865
  5. Broughton CE, van den Berg HA, Wemyss AM, Roper DI, Rodger A. (2016) Beyond the Discovery Void: New targets for antibacterial compounds. Science Progress. 99(2) 153-182
  6. Usha V, Lloyd AJ, Roper DI, Dowson CG, Kozlov G, Gehring K, Chauhan S, Imam HT, Blindauer CA, Besra GS. (2016) Reconstruction of diaminopimelic acid biosynthesis allows characterisation of Mycobacterium tuberculosis N-succinyl-L,L-diaminopimelic acid desuccinylase. Scientific Reports. 6: 23191 doi: 10.1038/srep23191
  7. Kaner RA, Allison SJ, Faulkner AD, Phillips RM, Roper DI, Shepherd SL, Simpson DH, Waterfield NR, Scott P. (2016) Anticancer metallohelices: nanomolar potency and high selectivity. Chemical Science 7(2): 951-958
  8. Teo ACK, Roper DI. (2015) Core Steps of Membrane-Bound Peptidoglycan Biosynthesis: Recent Advances, Insight and Opportunities. Antibiotics-Basel 4(4): 495-520
  9. Zuegg J, Muldoon C, Adamson G, McKeveney D, Le Thanh G, Premraj R, Becker B, Cheng M, Elliott AG, Huang JX, Butler MS, Bjaj M, Seifert J, Singh L, Galley NF, Roper DI, Lloyd AJ, Dowson CG, Cheng TJ, Cheng WC, Demon D, Meyer E, Meutermans W, Cooper MA. (2015) Carbohydrate scaffolds as glycosyltransferase inhibitors with in vivo antibacterial activity. Nature Communications. 6: 7719 doi:10.1038/ncomms8719
  10. Dow CE, van den Berg HA, Roper DI, Rodger A. (2015) Biological Insights from a Simulation Model of the Critical FtsZ Accumulation Required for Prokaryotic Cell Division. Biochemistry. 54(24): 3803-3813
  11. Broughton CE, Roper DI, van den Berg HA, Rodger, A. (2015) Bacterial cell division: experimental and theoretical approaches to the divisome. Science Progress. 98(4): 313-345
  12. Faulkner AD, Kaner RA, Abdallah QMA, Clarkson G, Fox DJ, Gurnani P, Howsonm SE, Phillips RM, Roper DI, Simpson D, & Scott P. (2014) Asymmetric ‘triplex’ metallohelices with high and selective activity against cancer cells Nature Chemistry 6(9): 797-803
  13. Qiong L, Cheng W, Morlot C, Bai XH, Jiang JL, Roper DI, Vernet T, Chen Y, and Zhou CZ. (2014). Full length structure of the major autolysin LytA. Acta crystallographica section D, Structural Biology. 71: 1373-1381
  14. Rodolis MT, Mihalyi A, O’Reilly AM, Slikas J, Roper DI, Hancock REW, & Bugg TDH. (2014). Identification of a Novel Inhibition Site in Translocase MraY based upon the Site of Interaction with Lysis Protein E from Bacteriophage X174. Chembiochem. 15(9):1300-8
  15. Braddick D, Sandhu S, Roper DI, Chappell MJ, Bugg TDH. (2014) Observation of the time-course for peptidoglycan lipid II polymerisation by Staphylococcus aureus monofunctional transglycosylase (2014) Microbiology. 2014 May 23. pii: mic.0.079442-0. doi: 10.1099/mic.0.079442-0
  16. Galley NF, O’Reilly AM, & Roper DI. (2014) Prospects for novel inhibitors of peptidoglycan transglycosylases. Bioorg Chem. 2014 May 21. pii: S0045-2068(14)00038-8.
  17. Paulin S, Jamshad M, Dafforn T, Garcia-Lara J, Foster S, Galley NF, Roper DI, Rosado H, Taylor P. (2014) Surfactant-Free Purification of Membrane Protein Complexes from Bacteria: Application to the Penicillin Binding Protein Complex PBP2/PBP2a of Staphylococcus aureus. Nanotechnology. 2014 Jun 27;25(28):285101
  18. Ruane KM, Lloyd AJ, Fulop V, Dowson, CG, Barreteau H, Boniface A, Dementin S, Blanot D, Mengin-Lecreulx D, Gobec S, Dessen A, & Roper DI. (2013) J Biol Chem 46, 33439-33448.
  19. Meigh L, Rodgers TL, Cann MJ, Roper DI, and Dale N. (2013) CO2 directly modulates connexin 26 by formation of a carbamate bridge between subunits. (2013) eLife Nov 12;2:e01213. doi: 10.7554/eLife.01213
  20. Zapun A, Philippe J, Abrahams KA, Signor L, Roper DI, Breukink E, and Vernet T, (2013) In-vitro reconstitution of peptidoglycan assembly from the Gram-positive pathogen Streptococcus pneumonia” ACS Chemical Biology 8(12):2688-96.
  21. Lloyd AJ, Potter NJ, Fishwick CWG, Roper DI & Dowson CG. (2013) Adenosine Tetraphosphoadenosine Consumption Drives a Continuous ATP-Release Assay for Catalysis by Aminoacyl-tRNA Synthetases and other Adenylate forming Enzymes. ACS chemical Biology 8 (10), pp 2157–2163
  22. Valegard K, Iqbal A, Kershaw NJ, Ivison D, Genereux C, Dubus A, Blikstad C, Demetriades M, Hopkinson RJ, Lloyd AJ, Roper DI, Schofield CJ, Andersson I, & McDonough, MA. (2013) Structural and mechanistic studies of the orf12 gene product from the clavulanic acid biosynthesis pathway, Acta crystallographica. Section D, Biological crystallography 69, 1567-1579.
  23. Majce V, Ruane KM, Gobec S, Roper DI. (2013) Crystallization and preliminary X-ray analysis of a UDP-MurNAc-tripeptide D-alanyl-D-alanine-adding enzyme (PaMurF) from Pseudomonas aeruginosa. Acta cryst F 69:503-5.
  24. Roper DI & Tame, JRH. “Chapter 769-Penicillin binding Protein 4” in Handbook of proteolytic enzymes. (ed) Barrett, A. J., Rawlings, N. D., and Woessner, J. F. 3rd ed. Elsevier Academic Press, Amsterdam; London. (2013) pp 3472-3475.
  25. Pacheco-Gomez, R., Cheng, X., Hicks, M. R., Smith, C. J., Roper, D. I., Addinall, S., Rodger, A., and Dafforn, T. R. (2013), Tetramerization of ZapA is required for FtsZ bundling Biochem J 449, 795-802. (10%)
  26. Dow, C. E., Rodger, A., Roper, D. I., and van den Berg, H. A. (2013) A model of membrane contraction predicting initiation and completion of bacterial cell division, Integr Biol (Camb) 5, 778-795. (10%)
  27. Yoshida, H., Kawai, F., Obayashi, E., Akashi, S., Roper, D. I., Tame, J. R., and Park, S. Y. (2012) Crystal structures of penicillin-binding protein 3 (PBP3) from methicillin-resistant Staphylococcus aureus in the apo and cefotaxime-bound forms, Journal of molecular biology 423, 351-364. (20%)
  28. Turner, D. J., Portman, I., Dafforn, T. R., Rodger, A., Roper, D. I., Smith, C. J., and Turner, M. S. (2012). The Mechanics of FtsZ Fibers. (2012), Biophys J 102, 731-738. (10%)
  29. Pacheo-Gomez, R. Roper, D., Dafforn, T. & Rodger, A. (2011) The pH dependence of polymerization and bundling by the essential bacterial cytoskeletal protein FtsZ Plos One 6, e19369. (25%)
  30. Bugg, T.D.H., Braddick, D., Lloyd, A.J., Dowson, C.G. & Roper, D.I. (2011) Bacterial Cell Wall Assembly: Still an Attractive Antibacterial Target. Trends Biotechnol. 2011 Apr;29(4):167-73. (25%)
  31. Hattersley JG, Pérez-Velázquez J, Chappell MJ, Bearup D, Roper D, Dowson C, Bugg T, Evans ND. (2010) Indistinguishability and identifiability of kinetic models for the MurC reaction in peptidoglycan biosynthesis. Comput Methods Programs Biomed. (10%)
  32. Batson, S, Rea D., Fulop, V & Roper D.I. (2010) Crystallization and preliminary X-ray analysis of a D-alanyl-D-alanine ligase (EcDdlB) from Escherichia coli. Acta Cryst F 66(Pt 4):405-408. (25%)
  33. Kawai F, Clarke TB, Roper DI, Han GJ, Hwang KY, Unzai S, Obayashi E, Park SY, Tame JR. (2010) Crystal Structures of Penicillin-Binding Proteins 4 and 5 from Haemophilus influenzae. J Mol Biol. 396(3): 634-45 (25%)
  34. Usha, V., Dover, L. G., Roper, D. I., Futterer, K., and Besra, G. S. (2009) Structure of the diaminopimelate epimerase DapF from Mycobacterium tuberculosis, Acta Crystallogr D Biol Crystallogr 65, 383-387. (25%)
  35. Sova, M., Cadez, G., Turk, S., Majce, V., Polanc, S., Batson, S., Lloyd, A. J., Roper, D. I., Fishwick, C. W., and Gobec, S. (2009) Design and synthesis of new hydroxyethylamines as inhibitors of D-alanyl-D-lactate ligase (VanA) and D-alanyl-D-alanine ligase (DdlB), Bioorg Med Chem Lett 19, 1376-1379. (20%)
  36. Paradis-Bleau, C., Lloyd, A., Sanschagrin, F., Maaroufi, H., Clarke, T., Blewett, A., Dowson, C., Roper, D. I., Bugg, T. D., and Levesque, R. C. (2009) Pseudomonas aeruginosa MurE amide ligase: enzyme kinetics and peptide inhibitor, Biochem J 421, 263-272 (20%)
  37. Cressina, E., Lloyd, A. J., De Pascale, G., James Mok, B., Caddick, S., Roper, D. I., Dowson, C. G., and Bugg, T. D. (2009) Inhibition of tRNA-dependent ligase MurM from Streptococcus pneumoniae by phosphonate and sulfonamide inhibitors, Bioorg Med Chem 17, 3443-3455. (20%)
  38. Clarke, T. B., Kawai, F., Park, S. Y., Tame, J. R., Dowson, C. G., and Roper, D. I. (2009) Mutational analysis of the substrate specificity of Escherichia coli penicillin binding protein 4, Biochemistry 48, 2675-2683. (25%)
  39. Usha, V., Dover, L. G., Roper, D. L., and Besra, G. S. (2008) Characterization of Mycobacterium tuberculosis diaminopimelic acid epimerase: paired cysteine residues are crucial for racemization, FEMS Microbiol Lett 280, 57-63. . (20%)
  40. Rea, D., Hovington, R., Rakus, J. F., Gerlt, J. A., Fulop, V., Bugg, T. D., and Roper, D. I. (2008) Crystal structure and functional assignment of YfaU, a metal ion dependent class II aldolase from Escherichia coli K12, Biochemistry 47, 9955-9965. (30%)
  41. Lloyd, A. J., Gilbey, A. M., Blewett, A. M., De Pascale, G., El Zoeiby, A., Levesque, R. C., Catherwood, A. C., Tomasz, A., Bugg, T. D., Roper, D. I., and Dowson, C. G. (2008) Characterization of tRNA-dependent peptide bond formation by MurM in the synthesis of Streptococcus pneumoniae peptidoglycan, J Biol Chem 283, 6402-6417. .(20%)
  42. De Pascale, G., Lloyd, A. J., Schouten, J. A., Gilbey, A. M., Roper, D. I., Dowson, C. G., and Bugg, T. D. (2008) Kinetic characterization of lipid II-Ala:alanyl-tRNA ligase (MurN) from Streptococcus pneumoniae using semisynthetic aminoacyl-lipid II substrates, J Biol Chem 283, 34571-34579. (20%)
  43. Alderwick, L. J., Dover, L. G., Veerapen, N., Gurcha, S. S., Kremer, L., Roper, D. L., Pathak, A. K., Reynolds, R. C., and Besra, G. S. (2008) Expression, purification and characterisation of soluble GlfT and the identification of a novel galactofuranosyltransferase Rv3782 involved in priming GlfT-mediated galactan polymerisation in Mycobacterium tuberculosis, Protein Expr Purif 58, 332-341. (10%)
  44. Small, E., Marrington, R., Rodger, A., Scott, D. J., Sloan, K., Roper, D., Dafforn, T. R., and Addinall, S. G. (2007) FtsZ polymer-bundling by the Escherichia coli ZapA orthologue, YgfE, involves a conformational change in bound GTP, J Mol Biol 369, 210-221. (20%)
  45. Rea, D., Fulop, V., Bugg, T. D., and Roper, D. I. (2007) Structure and mechanism of HpcH: a metal ion dependent class II aldolase from the homoprotocatechuate degradation pathway of Escherichia coli, J Mol Biol 373, 866-876. (30%)
  46. Lysenko, E. S., Clarke, T. B., Shchepetov, M., Ratner, A. J., Roper, D. I., Dowson, C. G., and Weiser, J. N. (2007) Nod1 signalling overcomes resistance of S. pneumoniae to opsonophagocytic killing, PLoS Pathog 3, e118. (20%)
  47. Lee, S. C., Stoilova-McPhie, S., Baxter, L., Fulop, V., Henderson, J., Rodger, A., Roper, D. I., Scott, D. J., Smith, C. J., and Morgan, J. A. (2007) Structural characterisation of the insecticidal toxin XptA1, reveals a 1.15 MDa tetramer with a cage-like structure, J Mol Biol 366, 1558-1568. (20%)
  48. Izumi, A., Rea, D., Adachi, T., Unzai, S., Park, S. Y., Roper, D. I., and Tame, J. R. (2007) Structure and mechanism of HpcG, a hydratase in the homoprotocatechuate degradation pathway of Escherichia coli, J Mol Biol 370, 899-911. (50%)
  49. Cressina, E., Lloyd, A. J., De Pascale, G., Roper, D. I., Dowson, C. G., and Bugg, T. D. (2007) Adenosine phosphonate inhibitors of lipid II: alanyl tRNA ligase MurM from Streptococcus pneumoniae, Bioorg Med Chem Lett 17, 4654-4656. (20%)
  50. Usha, V., Dover, L. G., Roper, D. L., Lloyd, A. J., and Besra, G. S. (2006) Use of a codon alteration strategy in a novel approach to cloning the Mycobacterium tuberculosis diaminopimelic acid epimerase, FEMS Microbiol Lett 262, 39-47. (20%)
  51. Totemeyer, S., Sheppard, M., Lloyd, A., Roper, D., Dowson, C., Underhill, D., Murray, P., Maskell, D., and Bryant, C. (2006) IFN-gamma enhances production of nitric oxide from macrophages via a mechanism that depends on nucleotide oligomerization domain-2, J Immunol 176, 4804-4810. (20%)
  52. Schouten, J. A., Bagga, S., Lloyd, A. J., de Pascale, G., Dowson, C. G., Roper, D. I., and Bugg, T. D. (2006) Fluorescent reagents for in vitro studies of lipid-linked steps of bacterial peptidoglycan biosynthesis: derivatives of UDPMurNAc-pentapeptide containing d-cysteine at position 4 or 5, Mol Biosyst 2, 484-491. (10%)
  53. Kishida, H., Unzai, S., Roper, D. I., Lloyd, A., Park, S. Y., and Tame, J. R. (2006) Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics, Biochemistry 45, 783-792. (30%)
  54. Bugg, T. D., Lloyd, A. J., and Roper, D. I. (2006) Phospho-MurNAc-pentapeptide translocase (MraY) as a target for antibacterial agents and antibacterial proteins, Infect Disord Drug Targets 6, 85-106. (20%)
  55. Adachi, T., Izumi, A., Rea, D., Park, S. Y., Tame, J. R., and Roper, D. I. (2006) Expression, purification and crystallization of 2-oxo-hept-4-ene-1,7-dioate hydratase (HpcG) from Escherichia coli C, Acta Crystallogr Sect F Struct Biol Cryst Commun 62, 1010-1012. (50%)
  56. Saidijam, M., Bettaney, K. E., Szakonyi, G., Psakis, G., Shibayama, K., Suzuki, S., Clough, J. L., Blessie, V., Abu-Bakr, A., Baumberg, S., Meuller, J., Hoyle, C. K., Palmer, S. L., Butaye, P., Walravens, K., Patching, S. G., O'Reilly, J., Rutherford, N. G., Bill, R. M., Roper, D. I., Phillips-Jones, M. K., and Henderson, P. J. (2005) Active membrane transport and receptor proteins from bacteria, Biochem Soc Trans 33, 867-872. (5%)
  57. Rodger, A., Marrington, R., Roper, D., and Windsor, S. (2005) Circular dichroism spectroscopy for the study of protein-ligand interactions, Methods Mol Biol 305, 343-364. (10%)
  58. Rea, D., Fulop, V., Bugg, T. D., and Roper, D. I. (2005) Expression, purification and preliminary crystallographic analysis of 2,4-dihydroxy-hepta-2-ene-1,7-dioate aldolase (HpcH) from Escherichia coli C, Acta Crystallogr Sect F Struct Biol Cryst Commun 61, 821-824. (30%)
  59. Chen, H. A., Simpson, P., Huyton, T., Roper, D., and Matthews, S. (2005) Solution structure and interactions of the Escherichia coli cell division activator protein CedA, Biochemistry 44, 6738-6744. (20%)
  60. Besong, G. E., Bostock, J. M., Stubbings, W., Chopra, I., Roper, D. I., Lloyd, A. J., Fishwick, C. W., and Johnson, A. P. (2005) A de novo designed inhibitor of D-Ala-D-Ala ligase from E. coli, Angew Chem Int Ed Engl 44, 6403-6406. (20%)
  61. Addinall, S. G., Johnson, K. A., Dafforn, T., Smith, C., Rodger, A., Gomez, R. P., Sloan, K., Blewett, A., Scott, D. J., and Roper, D. I. (2005) Expression, purification and crystallization of the cell-division protein YgfE from Escherichia coli, Acta Crystallogr Sect F Struct Biol Cryst Commun 61, 305-307. (30%)
  62. Rodger, A.; Marrington, R.; Roper, D.I.; and Windsor, S. “Circular dichroism spectroscopy for the study of protein ligand interactions” in Protein–Ligand Interactions: Methods and Protocols, Uli Nienhaus (ed) in Methods in Molecular Biology / Methods in Molecular Medicine The Humana Press Inc., New Jersey (2005): 305:343-364. (20%)
  63. Vevodova, J., Graham, R. M., Raux, E., Schubert, H. L., Roper, D. I., Brindley, A. A., Ian Scott, A., Roessner, C. A., Stamford, N. P., Elizabeth Stroupe, M., Getzoff, E. D., Warren, M. J., and Wilson, K. S. (2004) Structure/function studies on a S-adenosyl-L-methionine-dependent uroporphyrinogen III C methyltransferase (SUMT), a key regulatory enzyme of tetrapyrrole biosynthesis, J Mol Biol 344, 419-433. (20%)
  64. Lloyd, A. J., Huyton, T., Turkenburg, J., and Roper, D. I. (2004) Refinement of Haemophilus influenzae diaminopimelic acid epimerase (DapF) at 1.75 A resolution suggests a mechanism for stereocontrol during catalysis, Acta Crystallogr D Biol Crystallogr 60, 397-400. (50%)
  65. Blewett, A. M., Lloyd, A. J., Echalier, A., Fulop, V., Dowson, C. G., Bugg, T. D., and Roper, D. I. (2004) Expression, purification, crystallization and preliminary characterization of uridine 5'-diphospho-N-acetylmuramoyl L-alanyl-D-glutamate:lysine ligase (MurE) from Streptococcus pneumoniae 110K/70, Acta Crystallogr D Biol Crystallogr 60, 359-361. (30%)
  66. Willems, R. J., Top, J., Smith, D. J., Roper, D. I., North, S. E., and Woodford, N. (2003) Mutations in the DNA mismatch repair proteins MutS and MutL of oxazolidinone-resistant or -susceptible Enterococcus faecium, Antimicrob Agents Chemother 47, 3061-3066. (10%)
  67. Pudney, P. D., Buckley, S. L., Sidebottom, C. M., Twigg, S. N., Sevilla, M. P., Holt, C. B., Roper, D., Telford, J. H., McArthur, A. J., and Lillford, P. J. (2003) The physico-chemical characterization of a boiling stable antifreeze protein from a perennial grass (Lolium perenne), Arch Biochem Biophys 410, 238-245. (10%)
  68. Wright, A., Blewett, A., Fulop, V., Cooper, R., Burrows, S., Jones, C., and Roper, D. (2002) Expression, purification, crystallization and preliminary characterization of an HHED aldolase homologue from Escherichia coli K12, Acta Crystallogr D Biol Crystallogr 58, 2191-2193. (30%)
  69. Tame, J. R., Namba, K., Dodson, E. J., and Roper, D. I. (2002) The crystal structure of HpcE, a bifunctional decarboxylase/isomerase with a multifunctional fold, Biochemistry 41, 2982-2989. (30%)
  70. Cox, R. J., Durston, J., and Roper, D. I. (2002) Synthesis and in vitro enzyme activity of an oxa analogue of azi-DAP, Journal of the Chemical Society-Perkin Transactions 1, 1029-1035. (30%)
  71. Antson, A. A., Smith, D. J., Roper, D. I., Lewis, S., Caves, L. S., Verma, C. S., Buckley, S. L., Lillford, P. J., and Hubbard, R. E. (2001) Understanding the mechanism of ice binding by type III antifreeze proteins, J Mol Biol 305, 875-889. (20%)
  72. Roper, D. I., Huyton, T., Vagin, A., and Dodson, G. (2000) The molecular basis of vancomycin resistance in clinically relevant Enterococci: crystal structure of D-alanyl-D-lactate ligase (VanA), Proc Natl Acad Sci U S A 97, 8921-8925. (80%)
  73. Healy, V. L., Lessard, I. A., Roper, D. I., Knox, J. R., and Walsh, C. T. (2000) Vancomycin resistance in enterococci: reprogramming of the D-ala-D-Ala ligases in bacterial peptidoglycan biosynthesis, Chem Biol 7, R109-119. (30%)
  74. Major, G. N., Notarianni, G. B., Ross, S. J., Case, M. C., Brannigan, J. A., Roper, D. I., Potter, P. M., Brent, T. P., and Moody, P. C. E. (1999) Evidence for autoproteolysis of substrate-inactivated O-6-methylguanine-DNA methyltransferase following DNA repair, British Journal of Cancer 81, 576-576. (20%)
  75. Huyton, T., and Roper, D. I. (1999) Crystallization and preliminary X-ray characterization of VanA from Enterococcus faecium BM4147: towards the molecular basis of bacterial resistance to the glycopeptide antibiotic vancomycin, Acta Crystallogr D Biol Crystallogr 55, 1481-1483. (50%)
  76. Gardiner, L. P., Roper, D. I., Hammonds, T. R., and Maxwell, A. (1998) The N-terminal domain of human topoisomerase II alpha is a DNA-dependent ATPase, Biochemistry 37, 16997-17004. (50%)
  77. Subramanya, H. S., Roper, D. I., Dauter, Z., Dodson, E. J., Davies, G. J., Wilson, K. S., and Wigley, D. B. (1996) Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases, Biochemistry 35, 792-802. (50%)
  78. Jervis, T. J., Roper, D. I., and Glover, I. D. (1996) Crystallization and preliminary X-ray analysis of a bifunctional enzyme: HHDD isomerase/OPET decarboxylase from Escherichia coli, Acta Crystallogr D Biol Crystallogr 52, 1036-1038. (50%)
  79. Roper, D. I., Stringfellow, J. M., and Cooper, R. A. (1995) Sequence of the hpcC and hpcG genes of the meta-fission homoprotocatechuic acid pathway of Escherichia coli C: nearly 40% amino-acid identity with the analogous enzymes of the catechol pathway, Gene 156, 47-51. (80%)
  80. Roper, D. I., Subramanya, H. S., Shingler, V., and Wigley, D. B. (1994) Preliminary crystallographic analysis of 4-oxalocrotonate tautomerase reveals the oligomeric structure of the enzyme, J Mol Biol 243, 799-801. (80%)
  81. Cameron, A. D., Roper, D. I., Moreton, K. M., Muirhead, H., Holbrook, J. J., and Wigley, D. B. (1994) Allosteric activation in Bacillus stearothermophilus lactate dehydrogenase investigated by an X-ray crystallographic analysis of a mutant designed to prevent tetramerization of the enzyme, J Mol Biol 238, 615-625. (50%)
  82. Roper, D. I., Fawcett, T., and Cooper, R. A. (1993) The Escherichia coli C homoprotocatechuate degradative operon: hpc gene order, direction of transcription and control of expression, Mol Gen Genet 237, 241-250. (80%)
  83. Roper, D. I., and Cooper, R. A. (1993) Purification, nucleotide sequence and some properties of a bifunctional isomerase/decarboxylase from the homoprotocatechuate degradative pathway of Escherichia coli C, Eur J Biochem 217, 575-580. (80%)
  84. Roper, D. I., Moreton, K. M., Wigley, D. B., and Holbrook, J. J. (1992) The structural consequences of exchanging tryptophan and tyrosine residues in B. stearothermophilus lactate dehydrogenase, Protein Eng 5, 611-615. (80%)
  85. Roper, D. I., and Cooper, R. A. (1990) Purification, some properties and nucleotide sequence of 5-carboxymethyl-2-hydroxymuconate isomerase of Escherichia coli C, FEBS Lett 266, 63-66. (80%)
  86. Roper, D. I., and Cooper, R. A. (1990) Subcloning and nucleotide sequence of the 3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase gene from Escherichia coli C, FEBS Lett 275, 53-57. (80%)
  87. Wigley, D. B., Roper, D. I., and Cooper, R. A. (1989) Preliminary crystallographic analysis of 5-carboxymethyl-2-hydroxymuconate isomerase from Escherichia coli, J Mol Biol 210, 881-882 (80%)