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排序方式: 共有977条查询结果,搜索用时 156 毫秒
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Herwig Prasch Dr. Andreas Wolfsgruber Dr. Martin Thonhofer André Culum Christoph Mandl Dr. Patrick Weber Melanie Zündel Dr. Seyed A. Nasseri Dr. Andres Gonzalez Santana Dr. Gregor Tegl Prof. Dr. Bernd Nidetzky Prof. Dr. Karl Gruber Prof. Dr. Arnold E. Stütz Prof. Dr. Stephen G. Withers Prof. Dr. Tanja M. Wrodnigg 《Chembiochem : a European journal of chemical biology》2023,24(23):e202300480
Selective covalent labelling of enzymes using small molecule probes has advanced the scopes of protein profiling. The covalent bond formation to a specific target is the key step of activity-based protein profiling (ABPP), a method which has become an indispensable tool for measuring enzyme activity in complex matrices. With respect to carbohydrate processing enzymes, strategies for ABPP so far involve labelling the active site of the enzyme, which results in permanent loss of activity. Here, we report in a proof of concept study the use of ligand-directed chemistry (LDC) for labelling glycoside hydrolases near – but not in – the active site. During the labelling process, the competitive inhibitor is cleaved from the probe, departs the active site and the enzyme maintains its catalytic activity. To this end, we designed a building block synthetic concept for small molecule probes containing iminosugar-based reversible inhibitors for labelling of two model β-glucosidases. The results indicate that the LDC approach can be adaptable for covalent proximity labelling of glycoside hydrolases. 相似文献
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MSc. Bettina Motycka Dr. Florian Csarman Melanie Rupp Karoline Schnabel Gabor Nagy MSc. Kwankao Karnpakdee Stefan Scheiblbrandner Dr. Rupert Tscheliessnig Prof. Chris Oostenbrink Michal Hammel Assoc. Prof. Roland Ludwig 《Chembiochem : a European journal of chemical biology》2023,24(22):e202300431
The function of cellobiose dehydrogenase (CDH) in biosensors, biofuel cells, and as a physiological redox partner of lytic polysaccharide monooxygenase (LPMO) is based on its role as an electron donor. Before donating electrons to LPMO or electrodes, an interdomain electron transfer from the catalytic FAD-containing dehydrogenase domain to the electron shuttling cytochrome domain of CDH is required. This study investigates the role of two crucial amino acids located at the dehydrogenase domain on domain interaction and interdomain electron transfer by structure-based engineering. The electron transfer kinetics of wild-type Myriococcum thermophilum CDH and its variants M309A, R698S, and M309A/R698S were analyzed by stopped-flow spectrophotometry and structural effects were studied by small-angle X-ray scattering. The data show that R698 is essential to pull the cytochrome domain close to the dehydrogenase domain and orient the heme propionate group towards the FAD, while M309 is an integral part of the electron transfer pathway – its mutation reducing the interdomain electron transfer 10-fold. Structural models and molecular dynamics simulations pinpoint the action of these two residues on the domain interaction and interdomain electron transfer. 相似文献
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