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- W1973606909 abstract "The three-dimensional structures of endo-1,4-xylanase II (XYNII) from Trichoderma reesei complexed with 4,5-epoxypentyl beta-D-xyloside (X-O-C5),3,4-epoxybutyl beta-D-xyloside (X-O-C4), and 2,3-epoxypropyl beta-D-xyloside (X-O-C3) were determined by X-ray crystallography. High-resolution measurement revealed clear electron densities for each ligand. Both X-O-C5 and X-O-C3 were found to form a covalent bond with the putative nucleophile Glu86. Unexpectedly, X-O-C4 was found to bind to the putative acid/base catalyst Glu177. In all three complexes, clear conformational changes were found in XYNII compared to the native structure. These changes were largest in the X-O-C3 complex structure." @default.
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- W1973606909 date "1996-01-01" @default.
- W1973606909 modified "2023-09-26" @default.
- W1973606909 title "Covalent Binding of Three Epoxyalkyl Xylosides to the Active Site of <i>endo</i>-1,4-Xylanase II from <i>Trichoderma reesei</i><sup>,</sup>" @default.
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- W1973606909 doi "https://doi.org/10.1021/bi953052n" @default.
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