A mechanistic study of sialic acid mutarotation: implications for mutarotase enzymes

Org Biomol Chem. 2011 Jul 7;9(13):4818-22. doi: 10.1039/c1ob05079f. Epub 2011 May 17.

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, k(H2O)/k(D2O) = 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.

MeSH terms

  • Carbohydrate Epimerases / metabolism*
  • Micromonospora / enzymology*
  • Molecular Structure
  • N-Acetylneuraminic Acid / chemistry*
  • N-Acetylneuraminic Acid / metabolism
  • Substrate Specificity

Substances

  • Carbohydrate Epimerases
  • aldose 1-epimerase
  • N-Acetylneuraminic Acid