Direct Experimental Evidence for the High Chemical Reactivity of α- and β-Xylopyranosides Adopting a 2,5B Conformation in Glycosyl Transfer

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The complete conformational free energy landscape of β-xylose reveals a two-fold catalytic itinerary for β-xylanases.

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Q55325892-068B5DBA-E1EF-459F-8CF8-BACF0526B9C8

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Direct Experimental Evidence for the High Chemical Reactivity of α- and β-Xylopyranosides Adopting a 2,5B Conformation in Glycosyl Transfer

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http://www.wikidata.org/entity/Q57515384

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im Mai 2011 veröffentlichter wissenschaftlicher Artikel

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wetenschappelijk artikel

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наукова стаття, опублікована в травні 2011

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Direct Experimental Evidence f ...... formation in Glycosyl Transfer

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Direct Experimental Evidence f ...... formation in Glycosyl Transfer

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Direct Experimental Evidence f ...... formation in Glycosyl Transfer

@en

Direct Experimental Evidence f ...... formation in Glycosyl Transfer

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Direct Experimental Evidence f ...... formation in Glycosyl Transfer

@en

Direct Experimental Evidence f ...... formation in Glycosyl Transfer

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Direct experimental evidence f ...... formation in glycosyl transfer

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Jérôme Marrot

http://www.w3.org/2001/XMLSchema#string

Lidia Nieto

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Luis Amorim

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Mikael Bols

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Yves Blériot

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P2860

Sugar ring distortion in the glycosyl-enzyme intermediate of a family G/11 xylanase

Catalysis and specificity in enzymatic glycoside hydrolysis: a 2,5B conformation for the glycosyl-enzyme intermediate revealed by the structure of the Bacillus agaradhaerens family 11 xylanase

Structural and biochemical evidence for a boat-like transition state in beta-mannosidases

Stereoelectronic substituent effects.

Going to extremes: "super" armed glycosyl donors in glycosylation chemistry.

Mechanistic insights into glycosidase chemistry.

New principles for glycoside-bond formation.

Computational studies of the role of glycopyranosyl oxacarbenium ions in glycobiology and glycochemistry.

Oligosaccharide binding to family 11 xylanases: both covalent intermediate and mutant product complexes display (2,5)B conformations at the active centre.

Substrate specificity in glycoside hydrolase family 10. Tyrosine 87 and leucine 314 play a pivotal role in discriminating between glucose and xylose binding in the proximal active site of Pseudomonas cellulosa xylanase 10A.

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7345-7356

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scholarly article

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10.1002/CHEM.201003251

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English

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http://www.w3.org/2001/XMLSchema#string

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http://www.w3.org/2001/XMLSchema#string

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Jesus Jimenez-barbero

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2011-05-12T00:00:00Z

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21567492

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Direct Experimental Evidence for the High Chemical Reactivity of α- and β-Xylopyranosides Adopting a 2,5B Conformation in Glycosyl Transfer

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P2860

P2860

Direct Experimental Evidence for the High Chemical Reactivity of α- and β-Xylopyranosides Adopting a 2,5B Conformation in Glycosyl Transfer

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type

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P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698