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Study on the Enantioselectivity Inhibition Mechanism of Acetyl-Coenzyme A Carboxylase Toward Haloxyfop by Homology Modeling and MM-PBSA Analysis

Study on the Enantioselectivity Inhibition Mechanism of Acetyl-Coenzyme A Carboxylase Toward Haloxyfop by Homology Modeling and MM-PBSA Analysis

Jin Tao, Guirong Zhang, Aijun Zhang, Liangyu Zheng, Shugui Cao

J Mol Model. 2012 Aug;18(8):3783-92.

PMID: 22395649

Abstract:

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP69806344	Haloxyfop		69806-34-4	Price

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