Bacterial degradation of strobilurin fungicides

a role for a promiscuous methyl esterase activity of the subtilisin proteases?

Brook Clinton, Andrew C. Warden, Stephanie Haboury, Christopher J. Easton, Steven Kotsonis, Matthew C. Taylor, John G. Oakeshott, Robyn J. Russell, Colin Scott*

*Corresponding author for this work

Research output: Contribution to journalArticle

15 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)119-129
Number of pages11
JournalBiocatalysis and Biotransformation
Volume29
Issue number4
DOIs
Publication statusPublished - 2011
Externally publishedYes

Keywords

  • methyl esterase
  • trifloxystrobin
  • azoxystrobin

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