Lipase activity from Aspergillus fumigatus (AFL) were modulated by an effector (HMD) that was discovered for an allosteric site on the bioactive macromolecule. Experimental evaluation and computational modeling of allosteric effects revealed alterations in the structure of AFL. It was found that AFL's activity in HMD solution increased by approximately 46 % due to mainly enhanced lid flexibility. HMD-AFL interaction was driven by enthalpy and entropy. However, when AFL was coupled to HMD-modified microspheres (PS-HMD-p), its hydrolysis activity decreased by ∼14.3 % due to reduced lid flexibility. After immobilization, AFL's ester-synthesis activity also decreased, due to changes in the conformational dynamics and the geometric characteristics of active site. Investigating the structural dynamics of allosteric regulation of the lipase not only reveals its structural changes underlying the functional variation but also enhances the understanding of the allosteric property that is underappreciated in exoenzymes.
Keywords: Allosteric regulation; Lipase; Screening cascade; Structure.
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