title: The K1 beta-lactamase of Klebsiella pneumoniae.
abstract: 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.
authors.forename: B
authors.initials: B
authors.lastname: Joris
authors.forename: F
authors.initials: F
authors.lastname: De Meester
authors.forename: M
authors.initials: M
authors.lastname: Galleni
authors.forename: J M
authors.initials: JM
authors.lastname: Frère
authors.forename: J
authors.initials: J
authors.lastname: Van Beeumen
mesh_terms: D000596:Amino Acids / Q000032:analysis; D001665:Binding Sites; D007700:Kinetics; D007711:Klebsiella pneumoniae / Q000201:enzymology*; D010405:Penicillinase / Q000378:metabolism*; D010446:Peptide Fragments / Q000302:isolation & purification; D010449:Peptide Mapping; D013056:Spectrophotometry, Ultraviolet; D013438:Sulfhydryl Compounds / Q000032:analysis
chemical_list: D000596:Amino Acids; D010446:Peptide Fragments; D013438:Sulfhydryl Compounds; D010405:Penicillinase