Organism | UniProt | Comment | Textmining |
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synthetic construct | - |
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Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
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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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