Quantification of Enzymatic Biofilm Removal Using the Sauerbrey Equation: Application to the Case of .

A methodology for the quantitative analysis of enzymatic removal of biofilms (BF) was developed, based on a quartz crystal microbalance (QCM) under stationary conditions. This was applied to the case of (PP) BFs, through a series of five enzymes, whose removal activity was screened using the presented methodology. The procedure is based on the following: when BFs can be modeled as rigid materials, QCM can be used as a balance under stationary conditions for determining the BFs mass reduction by enzymatic removal.

Differential inhibition of homotrimeric dUTPases by the 3'-azido derivative of dideoxy-UTP.

The inhibitory effects of 3'-azido-2',3'-dideoxyuridine-5'-triphosphate in complex with the Mg2+ ion (azido-ddUTP.Mg) on the dUTPases of the human, E. coli, and equine infectious anemia virus have been compared.

A double role for a strictly conserved serine: further insights into the dUTPase catalytic mechanism.

Ser72 at the active site of the Escherichia coli dUTPase has been mutated to an alanine, and the properties of the mutant have been investigated. The serine is absolutely conserved among the monomeric and trimeric dUTPases (including the bifunctional dCTP deaminase:dUTPases), and it has been proposed to promote catalysis by balancing negative charge at the oxygen that bridges the alpha- and beta-phosphorus of the substrate. In all reported complexes of dUTPases with the substrate analogue alpha,beta-imido-dUTP.