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Bacterial degradation of strobilurin fungicides: a role for a promiscuous methyl esterase activity of the subtilisin proteases?

Clinton, Brook, Warden, Andrew C., Haboury, Stephanie, Easton, Christopher J., Kotsonis, Steven, Taylor, Matthew C., Oakeshott, John G., Russell, Robyn J., Scott, Colin·2011·Biocatalysis and Biotransformation

Abstract

Strobilurin fungicides are some of the most heavily used antifungal chemicals in agriculture. However, little is known of their fate in the environment. We have identified bacteria that slowly transform strobilurin fungicides via hydrolysis of a methyl ester group in the toxophore, rendering them non-fungicidal. A carboxypeptidase (subtilisin Carlsberg) was found to have this activity, albeit with low specific activity (2.4 × 10−2 nmol s−1 mg−1), and to possess specificity towards an analog of the fungicidal isomer of commercial strobilurins. Substrate-docking studies using the known structure for subtilisin Carlsberg revealed a plausible explanation for both the activity and isomer specificity of this class of hydrolase. These findings suggest that the promiscuous strobilurin methyl esterase activity of the subtilisin-like carboxypeptidases may have a role in the environmental fate of the strobilurin fungicides.

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Research works printed but not linked: 57

  1. Adetutu EM, 2008, J Appl Microbiol, 105, 1777, 10.1111/j.1365-2672.2008.03948.x · DOI
  2. Afriat L, 2006, Biochemistry, 45, 13677, 10.1021/bi061268r · DOI
  3. Anke T, 1977, J Antibiot, 30, 806, 10.7164/antibiotics.30.806 · DOI
  4. Anon, 1999, Metabolic pathways of agrochemicals Part 2: Insecticides and fungicides
  5. Anon, 2006, The pesticide manual
  6. Aunstrup K, 1969, U.S. Patent 3
  7. 10.1080/03601230701316465 · DOI
  8. Banerjee K, 2005, Anal Bioanal Chem, 382, 1527, 10.1007/s00216-005-3336-8 · DOI
  9. Banerjee K, 2006, J Agric Food Chem, 54, 9479, 10.1021/jf0620214 · DOI
  10. Banerjee K, 2007, Anal Bioanal Chem, 388, 1831, 10.1007/s00216-007-1382-0 · DOI
  11. Bartlett DW, 2002, Pest Manag Sci, 58, 649, 10.1002/ps.520 · DOI
  12. Becker WF, 1981, FEBS Lett, 132, 329, 10.1016/0014-5793(81)81190-8 · DOI
  13. Bending GD, 2006, Environ Pollut, 139, 279, 10.1016/j.envpol.2005.05.011 · DOI
  14. Brandt U, 1988, Eur J Biochem, 173, 499, 10.1111/j.1432-1033.1988.tb14026.x · DOI
  15. Brooks BR, 2009, J Comput Chem, 30, 1545, 10.1002/jcc.21287 · DOI
  16. Campbell PM, 1997, Biochem Genet, 35, 17, 10.1023/A:1022256412623 · DOI
  17. Chen J, 2008, J Agric Food Chem, 56, 1829, 10.1021/jf071527z · DOI
  18. Chen XH, 2009, J Biotechnol, 140, 27, 10.1016/j.jbiotec.2008.10.011 · DOI
  19. Copley SD, 2009, Nat Chem Biol, 5, 560, 10.1038/nchembio.197 · DOI
  20. Eschenburg S, 1998, Eur J Biochem, 257, 309, 10.1046/j.1432-1327.1998.2570309.x · DOI
  21. Ghosh RK, 2009, J Agric Food Chem, 57, 632, 10.1021/jf802716f · DOI
  22. Ghosh RK, 2009, Pest Manag Sci, 65, 1009, 10.1002/ps.1787 · DOI
  23. Hazato A, 1983, Nippon Kagaku Kaishi 1390–1392
  24. Horn JR, 2003, J Mol Biol, 331, 497, 10.1016/S0022-2836(03)00783-6 · DOI
  25. Horne I, 2002, Appl Environ Microbiol, 68, 3371, 10.1128/AEM.68.7.3371-3376.2002 · DOI
  26. Inouye K, 1992, J Biochem, 112, 335, 10.1093/oxfordjournals.jbchem.a123901 · DOI
  27. Jacobsen T, 1992, Can J Microbiol, 38, 75, 10.1139/m92-012 · DOI
  28. Kazlauskas RJ, 1991, J Org Chem, 56, 2656, 10.1021/jo00008a016 · DOI
  29. Khersonsky O, 2006, Curr Opin Chem Biol, 10, 498, 10.1016/j.cbpa.2006.08.011 · DOI · Paper page
  30. Kunst F, 1997, Nature, 390, 249, 10.1038/36786 · DOI · Paper page
  31. Ma YT, 1992, Biochemistry, 31, 11772, 10.1021/bi00162a014 · DOI
  32. Matsumae H, 1993, J Ferment Bioeng, 75, 93, 10.1016/0922-338X(93)90216-U · DOI
  33. 10.1271/bbb.63.1965 · DOI
  34. Momany FA, 1992, J Comput Chem, 13, 888, 10.1002/jcc.540130714 · DOI
  35. Mongodin EF, 2006, PLoS Genet, 2, 2094, 10.1371/journal.pgen.0020214 · DOI
  36. Morihara K, 1974, Arch Biochem Biophys, 165, 72, 10.1016/0003-9861(74)90143-X · DOI
  37. Nelson KE, 2002, Environ Microbiol, 4, 799, 10.1046/j.1462-2920.2002.00366.x · DOI
  38. Nobeli I, 2009, Nat Biotechnol, 27, 157, 10.1038/nbt1519 · DOI
  39. Patel SB, 1997, J Chem Technol Biotechnol, 69, 100, 10.1002/(SICI)1097-4660(199705)69:1<100::AID-JCTB675>3.0.CO;2-9 · DOI
  40. Peterson JD, 2001, Nucl Acid Res, 29, 123, 10.1093/nar/29.1.123 · DOI
  41. Philipp M, 1983, Mol Cell Biochem, 51, 5, 10.1007/BF00215583 · DOI
  42. Poupin P, 1999, J Bacteriol, 181, 3419, 10.1128/JB.181.11.3419-3426.1999 · DOI
  43. Rey MW, 2004, Genome Biol, 5, r77, 10.1186/gb-2004-5-10-r77 · DOI
  44. Robertus JD, 1972, Biochemistry, 11, 4293, 10.1021/bi00773a016 · DOI
  45. Russell RJ, 2011, Evol Appl, 4, 225, 10.1111/j.1752-4571.2010.00175.x · DOI · Paper page
  46. Sauter H, 1999, Angew Chem Int Ed, 38, 1329, 10.1002/(SICI)1521-3773(19990517)38:10<1328::AID-ANIE1328>3.0.CO;2-1 · DOI
  47. Scott C, 2008, Indian J Microbiol, 48, 65, 10.1007/s12088-008-0007-4 · DOI
  48. Scott C, 2009, Appl Environ Microbiol, 75, 2184, 10.1128/AEM.02634-08 · DOI
  49. Seki T, 1975, Int J Syst Bacteriol, 25, 258, 10.1099/00207713-25-3-258 · DOI
  50. 10.1080/03601230903471910 · DOI
  51. Squibb ER, 1968, U.S. Patent 3
  52. Tai DF, 1993, Biotechnol Lett, 15, 1229, 10.1007/BF00130302 · DOI
  53. Tyrell DJ, 1979, Appl Environ Microbiol, 38, 656, 10.1128/AEM.38.4.656-658.1979 · DOI
  54. Verma K, 2006, Ecotoxicol Environ Saf, 64, 377, 10.1016/j.ecoenv.2005.05.014 · DOI
  55. Wackett LP, 2009, Curr Opin Microbiol, 12, 244, 10.1016/j.mib.2009.05.001 · DOI
  56. Weir KM, 2006, Appl Environ Microbiol, 72, 3524, 10.1128/AEM.72.5.3524-3530.2006 · DOI
  57. Zhang Z, 2000, J Comput Biol, 7, 203, 10.1089/10665270050081478 · DOI

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Metadata

Authors
Clinton, B., Warden, A. C., Haboury, S., Easton, C. J., Kotsonis, S., Taylor, M. C., Oakeshott, J. G., Russell, R. J., & Scott, C.
Venue
Biocatalysis and Biotransformation
Published
2011-07-04
Volume
29
Issue
4
Pages
119-129
ISSN
  • 1024-2422
  • 1029-2446
Cited by
31
References
0
Language
en

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CoChat. (2026). Citation check: Bacterial degradation of strobilurin fungicides: a role for a promiscuous methyl esterase activity of the subtilisin proteases? https://app.cochat.ai/papers/10.3109/10242422.2011.578740
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Clinton, B., Warden, A. C., Haboury, S., Easton, C. J., Kotsonis, S., Taylor, M. C., Oakeshott, J. G., Russell, R. J., & Scott, C. (2011). Bacterial degradation of strobilurin fungicides: a role for a promiscuous methyl esterase activity of the subtilisin proteases? Biocatalysis and Biotransformation. https://doi.org/10.3109/10242422.2011.578740