ORBi: Jamin M. - Direct n.m.r. evidence for substrate-induced conformational changes in a beta-lactamase.

Reference : Direct n.m.r. evidence for substrate-induced conformational changes in a beta-lactamase.


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/77932

Title :	Direct n.m.r. evidence for substrate-induced conformational changes in a beta-lactamase.
Language :	English
Author, co-author :	Jamin, M. [> > > >]
	Damblon, Christian [Université de Liège - ULg > Département de chimie (sciences) > Chimie biologique structurale >]
	Bauduin-Misselyn, A. M. [> > > >]
	Durant, F. [> > > >]
	Roberts, G. C. [> > > >]
	Charlier, Paulette [Université de Liège - ULg > Département des sciences de la vie > Cristallographie des macromolécules biologiques >]
	Llabres, Gabriel [Université de Liège - ULg > Département de physique > Département de physique >]
	Frère, Jean-Marie [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Publication date :	1994
Journal title :	Biochemical Journal
Publisher :	Portland Press
Volume :	301 ( Pt 1)
Pages :	199-203
ISSN :	0264-6021
e-ISSN :	1470-8728
City :	London
Country :	United Kingdom
Keywords :	[en] Anti-Bacterial Agents ; Bacillus/enzymology ; Cefoxitin ; Circular Dichroism ; Crystallography ; Kinetics ; Magnetic Resonance Spectroscopy ; Protein Conformation ; Substrate Specificity ; beta-Lactamases/chemistry/metabolism
Abstract :	[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.
Permalink :	http://hdl.handle.net/2268/77932

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