Üretan hidrolazlarının parçacık tabanlı aktif-alan keşfi, çeşitli üretan bağlama modlarını ortaya koyuyor

Özet (abstract)

Abstract Recent advances in the discovery, characterisation, and engineering of urethanases provide new opportunities for the sustainable biocatalytic degradation of polyurethane waste. A mechanistic understanding of enzyme–plastic interactions is essential for structure-based engineering to enhance urethanase activity. However, the extremely complex and hydrophobic nature of polyurethane makes it challenging to elucidate the structural basis of enzyme–plastic interactions. Here, we used a fragment-based approach to characterise the active sites of two novel urethanases with different catalytic scaffolds, employing both a crystallographic fragment-screening (FASE) campaign and soluble fragments of plastic-like analogues that mimic the substrate, transition state, or product. FASE identified new substrate-binding subpockets while interactions of plastic mimetics in the active site provided a mechanistic understanding of the recognition and binding of polyurethane fragments by these subpockets. These results highlight a diversity of binding modes among urethanases toward different polyurethane fragments. Synopsis Fragment-based active site exploration of urethanases to elucidate polyurethane binding and cleavage

Yazarların özeti; kaynağından alınmıştır. Acta Crystallographica Section D Structural Biology, 2026 · DOI ↗