For the 9 enzymes that were not active against NIMS substrates, no detectable activity against any of the natural substrates was observed, again confirming the NIMS results.
As a result, we found that all tested hAID variants were active on 5 mC and had no detectable activity on 5 hmC.
In contrast, the N51A mutant had no detectable activity on any of the NNCN motifs.
Further validating the L. lactis system, we observed no detectable activity of AcrIIA2 against any Cas9 in this assay.
However, UGTPg102 and UGTPg103 were found to have no detectable activity on PPT.
On the other hand, the D77I mutant had no detectable activity toward phenolic acid methyl esters and feruloylated arabinoxylan.
However, the mismatched crHyb showed no detectable activity at any time point or concentration, demonstrating a much greater perturbation in catalytic activity.
Unexpectedly, the N51A mutant, with no detectable activity on C, exhibited robust, activity on 5 mC (~78% of the wt hAID activity).
Here, we report a class of highly selective MMP-13 inhibitors (pyrimidine dicarboxamides) that exhibit no detectable activity against other MMPs.
We observed that hAID exhibited a robust deaminase activity, the truncated mutant R190X was hyperactive and showed nearly 140% activity, R50A displayed approximately 20% activity, and N51A had no detectable activity (Fig. 1a c, upper panel).
Surprisingly, we found that the N51A hAID mutant, with no detectable activity on C, efficiently deaminated 5 mC, which may suggest different requirements for C and 5 mC deamination.
