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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
Kotsonis, Steven
Taylor, Matthew C
Oakeshott , John
Russell, Robyn J
Scott, Colin

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Informa Healthcare


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.



Keywords: Anti-fungal; Azoxystrobin; Bacterial degradation; Carboxypeptidase; Environmental fate; Esterase activities; Methyl esterase; Methyl esters; Specific activity; Strobilurin; Subtilisin; Subtilisin Carlsberg; Trifloxystrobin; Bacteriology; Enzymes; Esters; Azoxystrobin; Methyl esterase; Trifloxystrobin



Biocatalysis and Biotransformation


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