Substrate‐enzyme interactions and catalytic mechanism in a novel family VI esterase with dibutyl phthalate-hydrolyzing activity

Substrate Characterization for Hydrolysis of Multiple Types of Aromatic Esters by Promiscuous Aminopeptidases

“…The increasing trend in binding energies suggests that hydrogen bonding between aromatic esters and Aps may contribute to enhanced substrate hydrophobicity and reduced hydrophilicity, favoring the stabilization of the binding complex. 14,44 In parallel, the docking of PET monomer with Aps was illustrated in Figure S13I, and its docking binding energy was −9.9 kcal/mol, which was higher than that of Aps with aromatic esters. Structural analysis revealed that Aps has an α/β-hydrolases fold similar to that of PET hydrolase and the presence of a strictly conserved catalytic triad.…”

“…To gain a comprehensive understanding of the interaction mechanism, molecular docking techniques were employed, with a specific focus on elucidating the binding sites of aromatic esters within Aps (Figure S13). 14 In Table 2, the docking results revealed a trend in binding energies: BuPB (−6.5 kcal/mol) < DBP (−6.9 kcal/mol) < Fenpropathrin (−7.2 kcal/mol) < BzPB (−7.7 kcal/mol) = BBP (−7.7 kcal/ mol) < Cis-Cyfluthrin (−8.4 kcal/mol) = Deltamethrin (−8.4 kcal/mol) < Cypermethrin (−8.9 kcal/mol). The increasing trend in binding energies suggests that hydrogen bonding between aromatic esters and Aps may contribute to enhanced substrate hydrophobicity and reduced hydrophilicity, favoring the stabilization of the binding complex.…”

“…12,13 However, their viability and degradation efficiency in practical applications still exhibit certain limitations, falling short of meeting the demands. 14 In recent years, research on enzymatic degradation of aromatic esters has garnered widespread attention. Carboxylesterases are conventionally regarded as pivotal enzymes in the hydrolysis of aromatic esters, constituting the primary line of defense in the metabolism of endogenous compounds, pharmaceuticals, xenobiotics, and insecticides among other ester compounds.…”

Efficient removal of dibutyl phthalate from aqueous solutions: recent advances in adsorption and oxidation approaches

“…30–34 Microbial degradation represents a natural methodology that harnesses naturally occurring microorganisms and employs straightforward equipment. 35,36 It is environmentally friendly, but its effectiveness relies heavily on the microbial composition and environmental conditions. 37 Adsorption includes physical adsorption by electrostatic interactions, van der Waals forces, and surface tension, 38 and chemical adsorption relying on the affinity for the pollutant and the formation of new chemical bonds or complexes.…”

A Novel and Efficient Phthalate Hydrolase from Acinetobacter sp. LUNF3: Molecular Cloning, Characterization and Catalytic Mechanism

“…However, the relevant studies of PAE hydrolases mainly focus on gene cloning, function verification, catalytic characteristics and structure analysis. Although the catalytic mechanisms of dialkyl PAE hydrolase PS06828 and Hyd, from family VI and a new family, respectively, have been inferred from spectroscopic and docking analyses [ 24 , 27 ], only the catalytic triad of PS06828 (Ser113, Asp166 and His197) and key residues of Hyd (Thr190 and Ser191) are revealed. According to the results of molecular docking and enzyme assay, the interaction between MIBP and His399 affects the activity of GTW28_17760, a hydrolase from family VII capable of hydrolyzing DIBP and MIBP [ 20 ].…”