Reference : Direct n.m.r. evidence for substrate-induced conformational changes in a beta-lactamase.
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Direct n.m.r. evidence for substrate-induced conformational changes in a beta-lactamase.
Jamin, M. [> > > >]
Damblon, Christian mailto [Université de Liège - ULg > Département de chimie (sciences) > Chimie biologique structurale >]
Bauduin-Misselyn, A. M. [> > > >]
Durant, F. [> > > >]
Roberts, G. C. [> > > >]
Charlier, Paulette mailto [Université de Liège - ULg > Département des sciences de la vie > Cristallographie des macromolécules biologiques >]
Llabres, Gabriel mailto [Université de Liège - ULg > Département de physique > Département de physique >]
Frère, Jean-Marie mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Biochemical Journal
Portland Press
301 ( Pt 1)
Yes (verified by ORBi)
United Kingdom
[en] Anti-Bacterial Agents ; Bacillus/enzymology ; Cefoxitin ; Circular Dichroism ; Crystallography ; Kinetics ; Magnetic Resonance Spectroscopy ; Protein Conformation ; Substrate Specificity ; beta-Lactamases/chemistry/metabolism
[en] Cefoxitin and other beta-lactam antibiotics with a methoxy group on the alpha-face behave as very poor substrates of the Bacillus licheniformis beta-lactamase. The kinetic properties of the enzyme-cefoxitin system made it theoretically suitable for a detailed structural study of the acyl-enzyme. Unfortunately, soaking the crystals in cefoxitin solution did not allow detection of a crystalline acyl-enzyme complex. In contrast, direct observation by n.m.r. of the stable acyl-enzyme formed with cefoxitin and moxalactam indicated clear modifications of the enzyme structure, which were reflected in the aromatic and high-field methyl regions of the spectrum. The return to the initial free enzyme spectrum was concomitant with the hydrolysis of the acyl-enzyme, the process being slow enough to allow multidimensional n.m.r. experiments.

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