Esterases are crucial for aryloxyphenoxypropionate herbicide
(AOPP)
biodegradation. However, the underlying molecular mechanisms of AOPP
biodegradation by esterases are poorly understood. In the current
work, Corynebacterium sp. Z-1 was isolated and found
to degrade multiple AOPPs, including quizalofop-p-ethyl (QPE), haloxyfop-p-methyl (HPM), fenoxaprop-p-ethyl (FPE), cyhalofop-butyl (CYB), and clodinafop-propargyl
(CFP). A novel esterase, QfeH, which catalyzes the cleavage of ester
bonds in AOPPs to form AOPP acids, was identified from strain Z-1.
The catalytic activities of QfeH toward AOPPs decreased in the following
order: CFP > FPE > CYB > QPE > HPM. Molecular docking,
computational
analyses, and site-directed mutagenesis indicated the catalytic mechanisms
of QfeH-mediated degradation of different AOPPs. Notably, the key
residue S159 is essential for the activity of QfeH. Moreover, V222Y,
T227M, T227A, A271R, and M275K mutants, exhibiting 2.9–5.0
times greater activity than QfeH, were constructed. This study facilitates
the mechanistic understanding of AOPPs bioremediation by esterases.