  Design, implementation, and test of a digitally-controlled electrical power supply for the OUFTI-1 nanosatellite; ; et al Scientific conference (2010) Detailed reference viewed: 11 (0 ULg)OUFTI-1: New Student Nano-Satellite at ULg; ; Pisane, Jonathan  et alScientific conference (2008) Detailed reference viewed: 10 (2 ULg)OUFTI-1: The CubeSat developed at the University of Liège, Belgium; Pisane, Jonathan ; et alConference (2008) Detailed reference viewed: 11 (2 ULg)Unexpected Influence of a C-Terminal-Fused His-Tag on the Processing of an Enzyme and on the Kinetic and Folding Parameters; Duez, Colette ; et alin FEBS Letters (1997), 413(2), 194-6 The addition of a poly-His C-terminal extension, designed to facilitate the purification of the protein, to the beta-lactamase of a thermophilic Bacillus licheniformis strain modified the site of action ... [more ▼] The addition of a poly-His C-terminal extension, designed to facilitate the purification of the protein, to the beta-lactamase of a thermophilic Bacillus licheniformis strain modified the site of action of the signal peptidase. This resulted in the secretion of a protein with a different N-terminus, showing that this type of protein engineering might not always be as 'neutral' as generally assumed. [less ▲] Detailed reference viewed: 49 (16 ULg)Kinetic Study of Interaction between Brl 42715, Beta-Lactamases, and D-Alanyl-D-Alanine PeptidasesMatagne, André ; ; et alin Antimicrobial Agents and Chemotherapy (1995), 39(1), 227-31 A detailed kinetic study of the interactions between BRL 42715, a beta-lactamase-inhibiting penem, and various beta-lactamases (EC 3.5.2.6) and D-alanyl-D-alanine peptidases (DD-peptidases, EC 3.4.16.4 ... [more ▼] A detailed kinetic study of the interactions between BRL 42715, a beta-lactamase-inhibiting penem, and various beta-lactamases (EC 3.5.2.6) and D-alanyl-D-alanine peptidases (DD-peptidases, EC 3.4.16.4) is presented. The compound was a very efficient inactivator of all active-site serine beta-lactamases but was hydrolyzed by the class B, Zn(2+)-containing enzymes, with very different kcat values. Inactivation of the Streptomyces sp. strain R61 extracellular DD-peptidase was not observed, and the Actinomadura sp. strain R39 DD-peptidase exhibited a low level of sensitivity to the compound. [less ▲] Detailed reference viewed: 30 (3 ULg)Modelling of Accessibility FieldsDonnay, Jean-Paul ; in Proceeding of the First Joint European Conference on Geographical Information (1995) Detailed reference viewed: 17 (0 ULg)A comparative study of class-D beta-lactamases.; ; Joris, Bernard et alin Biochemical Journal (1993), 292 ( Pt 2) Three class-D beta-lactamases (OXA2, OXA1 and PSE2) were produced and purified to protein homogeneity. 6 beta-Iodopenicillanate inactivated the OXA2 enzyme without detectable turnover. Labelling of the ... [more ▼] Three class-D beta-lactamases (OXA2, OXA1 and PSE2) were produced and purified to protein homogeneity. 6 beta-Iodopenicillanate inactivated the OXA2 enzyme without detectable turnover. Labelling of the same beta-lactamase with 6 beta-iodo[3H]penicillanate allowed the identification of Ser-70 as the active-site serine residue. In agreement with previous reports, the apparent M(r) of the OXA2 enzyme as determined by molecular-sieve filtration, was significantly higher than that deduced from the gene sequence, but this was not due to an equilibrium between a monomer and a dimer. The heterogeneity of the OXA2 beta-lactamase on ion-exchange chromatography contrasted with the similarity of the catalytic properties of the various forms. A first overview of the enzymic properties of the three 'oxacillinases' is presented. With the OXA2 enzyme, 'burst' kinetics, implying branched pathways, seemed to prevail with many substrates. [less ▲] Detailed reference viewed: 8 (0 ULg) |
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