The Potential Binding Interaction and Hydrolytic Mechanism of Carbaryl with the Novel Esterase PchA in Pseudomonas sp. PS21
journal contributionposted on 11.02.2022, 13:03 authored by Zhiyan Jiang, Liwen Qu, Gaopeng Song, Jie Liu, Guohua Zhong
Microbial bioremediation is a very potent and eco-friendly approach to alleviate pesticide pollution in agricultural ecosystems, and hydrolase is an effective element for contaminant degradation. In the present study, a novel Mn2+-dependent esterase, PchA, that efficiently hydrolyzes carbamate pesticides with aromatic structures was identified from Pseudomonas sp. PS21. The hydrolytic activity was confirmed to be related closely to the core catalytic domain, which consists of six residues. The crucial residues indirectly stabilized the position of carbaryl via chelating Mn2+ according to the binding model clarified by molecular simulations, and the additional hydrophobic interactions between carbaryl with several hydrophobic residues also stabilized the binding conformation. The residue Glu398, by serving as the general base, might activate a water molecule and facilitate PchA catalysis. This work offers valuable insights into the binding interaction and hydrolytic mechanism of carbaryl with the hydrolase PchA and will be crucial to designing strategies leading to the protein variants that are capable of degrading related contaminants.
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designing strategies leadingcore catalytic domainalleviate pesticide pollutionadditional hydrophobic interactionsdegrading related contaminantsbinding model clarifiedfacilitate pcha catalysisps21 microbial bioremediationpotential binding interaction2 +</ supnovel esterase pchabinding interactionrelated closelynovel mnbinding conformationwater moleculesix residuesresidue glu398pseudomonas </protein variantspresent studymolecular simulationsmight activatehydrolytic mechanismhydrolytic activitygeneral basefriendly approacheffective elementcontaminant degradationaromatic structuresagricultural ecosystems