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- W2002072458 abstract "Three-dimensional structures of a sucrose isomerase from Pseudomonas mesoacidophila MX-45, forming mainly trehalulose have been solved to resolutions in the range 1.8–2.2 Å. Native and mutant complexes give, for the first time, a thorough insight into substrate binding and recognition, and product specificities of these enzymes. This study has pinpointed essential residues for binding the substrate sucrose, and hereby given detailed information on the interactions between the enzyme active site and glucosyl- and fructosyl moieties. Moreover, the 3-D structures revealed an aromatic clamp formed by two phenylalanines, which plays an essential role in recognition of the substrate and in controlling the reaction specificity." @default.
- W2002072458 created "2016-06-24" @default.
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- W2002072458 date "2008-01-01" @default.
- W2002072458 modified "2023-10-18" @default.
- W2002072458 title "Insights into sucrose isomerization from crystal structures of thePseudomonas mesoacidophilaMX-45 sucrose isomerase, MutB" @default.
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- W2002072458 doi "https://doi.org/10.1080/10242420701788694" @default.
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