The K1 beta-lactamase of Klebsiella pneumoniae

Biochem J. 1987 Apr 15;243(2):561-7. doi: 10.1042/bj2430561.

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / analysis
  • Binding Sites
  • Kinetics
  • Klebsiella pneumoniae / enzymology*
  • Penicillinase / metabolism*
  • Peptide Fragments / isolation & purification
  • Peptide Mapping
  • Spectrophotometry, Ultraviolet
  • Sulfhydryl Compounds / analysis

Substances

  • Amino Acids
  • Peptide Fragments
  • Sulfhydryl Compounds
  • Penicillinase