AI Article Synopsis
- A recombinant D92G mutant sialidase from Micromonospora viridifaciens was successfully cloned, expressed, and purified.
- Kinetic studies indicate that replacing the conserved aspartic acid with glycine results in a functional sialidase with notable activity against specific substrates, showing a significant free energy contribution to its hydrolysis process.
- Structural analysis reveals that the D92G mutation doesn't noticeably alter the active site arrangement, with a water molecule taking the place of the removed aspartic acid.
Article Abstract
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.
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| http://dx.doi.org/10.1016/j.febslet.2004.10.016 | DOI Listing |
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