Journal
JOURNAL OF MOLECULAR MODELING
Volume 18, Issue 8, Pages 3783-3792Publisher
SPRINGER
DOI: 10.1007/s00894-012-1387-2
Keywords
Acetyl-coenzyme A carboxylase; Enantioselective recognition mechanism; Haloxyfop, Homology modeling; MM-PBSA analysis
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Funding
- National Natural Science Foundation of China [20802025, 30870539, 20432010, 20672045]
- Jilin Provincial Science&Technology Sustentation Program [20110436]
- Jilin University
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Acetyl-coenzyme A carboxylase (ACCase) has been identified as one of the most important targets of herbicide Aryloxyphenoxypropionates (APPs). ACCase shows different enantioselectivity toward APPs, and only (R)-enantiomers of APPs have the herbicidal activity. In order to deeply understand the enantioselective recognition mechanism of ACCase, (R)-haloxyfop, which is a typical commercial herbicide from APPs, is selected and the relative binding free energy between ACCase and (R)-haloxyfop is investigated and compared with that between ACCase and (S)-haloxyfop by homology modeling and molecular mechanics-Poisson-Boltzmann surface area (MM-PBSA) method. Further free energy analysis reveals that the preference of ACCase toward (R)-haloxyfop is mainly driven by Van der Waals interaction. The analysis of the interaction between the active site residues of ACCase CT domain and (R)-haloxyfop shows the van der Waals interactions have a close relationship with the addition effect of each residue. An understanding of the enantioselective recognition mechanism between ACCase and haloxyfop is desirable to discover novel chiral herbicides.
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