Reference : The beta-lactamase of Enterobacter cloacae P99. Chemical properties, N-terminal sequence...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/124944
The beta-lactamase of Enterobacter cloacae P99. Chemical properties, N-terminal sequence and interaction with 6 beta-halogenopenicillanates.
English
Joris, Bernard mailto [Université de Liège - ULg > Département des sciences de la vie > Physiologie et génétique bactériennes]
De Meester, F [> > > >]
Galleni, Moreno mailto [Université de Liège - ULg > Département des sciences de la vie > Macromolécules biologiques]
Reckinger, G [> > > >]
Coyette, Jacques mailto [Université de Liège - ULg > Services généraux (Faculté des sciences) > Relations académiques et scientifiques (Sciences)]
Frère, Jean-Marie mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines]
Van Beeumen, J [> > > >]
1985
Biochemical Journal
Portland Press
228
1
241-8
Yes (verified by ORBi)
International
0264-6021
1470-8728
London
United Kingdom
[en] Amino Acid Sequence ; Amino Acids/analysis ; Enterobacter/enzymology ; Enterobacteriaceae/enzymology ; Kinetics ; Penicillanic Acid/metabolism ; Spectrophotometry ; Tryptophan/analysis ; beta-Lactamases/antagonists & inhibitors
[en] The beta-lactamase of Enterobacter cloacae P99 consists of one polypeptide chain of Mr 39000 devoid of disulphide bridges and free thiol groups. It contains an unusually high proportion of tyrosine and tryptophan. The N-terminal sequence exhibits overlaps with the tryptic peptide obtained after labelling the active site with 6 beta-iodopenicillanate. The active-site serine residue is at position 64. The homology with the chromosomal beta-lactamase of Escherichia coli K 12 (ampC gene) is lower within the 25 residues of the N-terminal portion than around the active-site serine residue. The P99 beta-lactamase is inactivated by 6 beta-bromo- and 6 beta-iodo-penicillanate, with a second-order rate constant of 110-140M-1 X s-1 at 30 degrees C and pH 7.0, a value that is much lower than that observed with class-A beta-lactamases.
http://hdl.handle.net/2268/124944

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