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5203748 
Journal Article 
Bacterial degradation of strobilurin fungicides: a role for a promiscuous methyl esterase activity of the subtilisin proteases? 
Clinton, B; Warden, AC; Haboury, S; Easton, CJ; Kotsonis, S; Taylor, MC; Oakeshott, JG; Russell, RJ; Scott, C 
2011 
Yes 
Biocatalysis and Biotransformation
ISSN: 1024-2422 
29 
4 
119-129 
WOS:000293121500003 
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 x 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. 
Methyl esterase; trifloxystrobin; azoxystrobin