By using the criterion of activity against 6,8-difluoro-4-methylumbelliferyl phosphate, all wild-type phosphatase complexes were found to be active, whereas the catalytically inactive PP4C mutants had negligible activity (supplementary Fig S2 online).
Most of the known DNA methyltransferases are catalytically active in the pH range of 7.0-8.5, but HP0593 MTase showed negligible activity in this pH range.
Samples treated with antibiotics and positive control alone showed negligible activity on biofilm prevention/inhibition.
PNP is highly specific for 6-oxopurine nucleosides and exhibits negligible activity for 6-aminopurine nucleosides.
This was rationalized by realizing the negligible activity of zeolite protons for NO NO2 equilibration.
In this study, whole-cell biotransformation showed that the un-induced strain CNP-8 exhibited negligible activity for 2C4NP.
Pectin methylesterase showed a negligible activity which is related to the confirmed presence of a pectin methylesterase inhibitor.
This showed that K/TiO2 displayed negligible activity due to the immobilization of K+ ions in TiO2 to form K2Ti6O13.
The bare electrode backbone shows negligible activity for propane oxidation, while in the presence of Pt nanoparticles a high catalytic activity is obtained above 200 °C.
A second double mutant, E223D/S271A, showed a 1.27-fold increased activity compared to the wild-type XR with NADPH and almost negligible activity with NADH.
3-O-sulfated GlcA was active against DENV infection, whereas 2-O-sulfated GlcA and 3,6-di-O-sulfated Glc showed negligible activity.
