Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5131807 | Analytical Biochemistry | 2017 | 4 Pages |
Abstract
We recently reported on the kinetics of the polygalacturonase TtGH28 acting on trimer and dimer substrates. When the starting substrate for hydrolysis is the trimer, the product dimer is also subject to hydrolysis, resulting in discrepancies when either the concentration of dimer or monomer product is used for analysis of trimer hydrolysis. Here, we derive a method for determining catalytic rates of exo-hydrolases acting on trimer (and higher order) substrates when products may also be substrates for hydrolysis and show how this correction may be applied for TtGH28.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
J. Rose Stoller, Kurt Wagschal, Charles C. Lee, Douglas B. Jordan,