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A recombinant D92G mutant sialidase from Micromonospora viridifaciens has been cloned, expressed and purified. Kinetic studies reveal that the replacement of the conserved aspartic acid with glycine results in a catalytically competent retaining sialidase that possesses significant activity against activated substrates. The contribution of this aspartate residue to the free energy of hydrolysis for natural substrates is greater than 19 kJ/mol. The three dimensional structure of the D92G mutant shows that the removal of aspartic acid 92 causes no significant re-arrangement of the active site, and that an ordered water molecule substitutes for the carboxylate group of D92.

Original publication

DOI

10.1016/j.febslet.2004.10.016

Type

Journal article

Journal

FEBS Lett

Publication Date

05/11/2004

Volume

577

Pages

265 - 269

Keywords

Aspartic Acid, Base Sequence, Binding Sites, Carbohydrate Sequence, Catalysis, DNA Primers, Magnetic Resonance Spectroscopy, Micromonospora, Neuraminidase