The K1 beta-lactamase of Klebsiella pneumoniae.
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.
Joris
B
B
De Meester
F
F
Galleni
M
M
Frère
J M
JM
Van Beeumen
J
J
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
D000596:Amino Acids; D010446:Peptide Fragments; D013438:Sulfhydryl Compounds; D010405:Penicillinase