Reference : The K1 beta-lactamase of Klebsiella pneumoniae.
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
The K1 beta-lactamase of Klebsiella pneumoniae.
Joris, Bernard mailto [Université de Liège - ULiège > Département des sciences de la vie > Physiologie et génétique bactériennes]
De Meester, F [> > > >]
Galleni, Moreno mailto [Université de Liège - ULiège > Département des sciences de la vie > Macromolécules biologiques]
Frère, Jean-Marie mailto [Université de Liège - ULiège > > Centre d'ingénierie des protéines]
Van Beeumen, J [> > > >]
Biochemical Journal
Portland Press
Yes (verified by ORBi)
United Kingdom
[en] Amino Acids/analysis ; Binding Sites ; Kinetics ; Klebsiella pneumoniae/enzymology ; Penicillinase/metabolism ; Peptide Fragments/isolation & purification ; Peptide Mapping ; Spectrophotometry, Ultraviolet ; Sulfhydryl Compounds/analysis
[en] beta-Lactamase K1 was purified from Klebsiella pneumoniae SC10436. It is very similar to the enzyme produced by Klebsiella aerogenes 1082E and described by Emanuel, Gagnon & Waley [Biochem. J. (1986) 234, 343-347]. An active-site peptide was isolated after labelling of the enzyme with tritiated beta-iodopenicillanate. A cysteine residue was found just before the active-site serine residue. This result could explain the properties of the enzyme after modification by thiol-blocking reagents. The sequence of the active-site peptide clearly established the enzyme as a class A beta-lactamase.

File(s) associated to this reference

Fulltext file(s):

Open access
Publi_BJ_18.pdfPublisher postprint3.22 MBView/Open

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.