Why catalytic residues mutants of GH5 enzyme still remain a lot activity ?

09 September 2019 0 1K Report

I have mutated the catalytic residues (nucleophile or acid/base) of a GH5-29 subfamily enzyme, which naturally use glycosphingolipids as substrate. Unexpectly, the mutants still remaining ~ 60% activity when use PNP-Gal as a substrate. My question is why the mutants still have activity, is it because the PNP-Gal have a good leaving group (PNP)?

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