Article
Bridging the Gap in the Structure-Function Paradigm of Enzymatic PET Degradation-Aromatic Residue Driven Balanced Interactions with Catalytic and Anchoring Subsite.
Chembiochem : a European journal of chemical biology - 4 Nov 2024
James Anjima, Bhasi Anjitha, De Susmita
Abstract excerpt
Understanding all parameters contributing to enzyme activity is crucial in enzyme catalysis. For enzymatic PET degradation, this involves examining the formation of the enzyme-PET complex. In IsPETase (WT), a PET-degrading enzyme from Ideonella sakaiensis, mutating two non-catalytic residues (DM) significantly enhances activity. Such mutations, depending on their position in the tertiary structure, fine-tune...
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