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available and catalytically competent active site, but most also possess favourable
secondary interactions counter within the active site. Enzymes possessing a prefer-
ence for hydrophobic aromatic amino acids have a greater capacity for hydrolyzing
PTMS and as such show enhanced hydrolysis rates. While a complete and accurate
reaction mechanism is debated, theoretical calculations suggest that the first step of
the mechanism proceeds through serine addition to the alkoxysilane.
Acknowledgements The authors would like to thank Razvan Simionescu (Brock University) for
assistance in acquiring NMR spectra. Funding for these projects was provided by Brock Univer-
sity, Natural Science and Engineering Research Council (NSERC), and the Ontario Partnership for
Industrialization and Commercialization (OPIC). MBF was supported through graduate scholar-
ships from the Ontario Scholarship (OGS), the Ontario Graduate Scholarship in Science and Tech-
nology (OGSST) and the Queen Elizabeth II Graduate Scholarship in Science and Technology
(QEII-GSST) programs.
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