The Structure of Sucrose-Soaked Levansucrase Crystals from Erwinia tasmaniensis reveals a Binding Pocket for Levanbiose.
作者： Ivan Polsinelli , Rosanna Caliandro , Nicola Demitri , Stefano Benini
DOI: 10.3390/IJMS21010083
关键词:
摘要: Given its potential role in the synthesis of novel prebiotics and applications pharmaceutical industry, a strong interest has developed enzyme levansucrase (LSC, EC 2.4.1.10). LSC catalyzes both hydrolysis sucrose (or sucroselike substrates) transfructosylation wide range acceptors. from Gram-negative bacterium Erwinia tasmaniensis (EtLSC) is an interesting biocatalyst due to high-yield production fructooligosaccharides (FOSs). In order learn more about process chain elongation, we obtained crystal structure EtLSC complex with levanbiose (LBS). LBS FOS intermediate formed during longer-chain FOSs levan. Analysis binding pocket revealed that was conserved several related species. The discovered this ideal target for future mutagenesis studies understand biological relevance engineer LSCs into tailored products.
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