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Issue 13, 2011
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A mechanistic study of sialic acid mutarotation: Implications for mutarotase enzymes

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Abstract

The mutarotation of N-acetylneuraminic acid (Neu5Ac) proceeds by four kinetically distinct pathways: (i) the acid-catalyzed reaction of neutral Neu5Ac; (ii) the spontaneous reaction of the carboxylic acid (the kinetically equivalent acid-catalyzed reaction on the anion being ruled out by the solvent deuterium kinetic isotope effect of 3.74 ± 0.68); (iii) a spontaneous, water-catalyzed, reaction of the anion; and (iv) a specific-base catalyzed reaction of the anion. The magnitude of the solvent kinetic isotope effect, kH2O/kD2O = 4.48 ± 0.74 is consistent with a ring-opening transition state in which a water molecule is deprotonating the anomeric hydroxyl group in concert with strengthening solvation of the ring oxygen atom. The mechanistic implications for Neu5Ac mutarotases are discussed.

Graphical abstract: A mechanistic study of sialic acid mutarotation: Implications for mutarotase enzymes

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Publication details

The article was received on 14 Jan 2011, accepted on 11 Apr 2011 and first published on 12 Apr 2011


Article type: Paper
DOI: 10.1039/C1OB05079F
Citation: Org. Biomol. Chem., 2011,9, 4818-4822
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    A mechanistic study of sialic acid mutarotation: Implications for mutarotase enzymes

    J. Chan, G. Sandhu and A. J. Bennet, Org. Biomol. Chem., 2011, 9, 4818
    DOI: 10.1039/C1OB05079F

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