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Literature summary for 3.2.1.25 extracted from

  • Ardevol, A.; Biarnes, X.; Planas, A.; Rovira, C.
    The conformational free-energy landscape of beta-D-mannopyranose: evidence for a 1S5 - B2,5 - OS2 catalytic itinerary in beta-mannosidases (2010), J. Am. Chem. Soc., 132, 16058-16065.
    View publication on PubMed
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Organism

Organism UniProt Comment Textmining
synthetic construct
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information calculation of conformational free-energy surface of a beta-D-mannopyranose molecule associated with the ideal Stoddart conformational diagram. 1S5 is among the most stable conformers and simultaneously is the most preactivated conformation in terms of elongation/shortening of the C1-O1/C1-O5 bonds, C1-O1 orientation, and charge development at the anomeric carbon. Analysis of the computed free-energy surface gives support to the proposed 1S5-B2,5-OS2 catalytic itinerary. The degree of preactivation of the substrate in glycoside hydrolases is related to the properties of an isolated sugar ring. Introduction of a simple preactivation index integrating several structural, electronic, and energetic properties that can be used to predict the conformation of the substrate in the Michaelis complex of any glycoside hydrolase synthetic construct ?
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