| Literature DB >> 3307765 |
B Joris, F De Meester, M Galleni, J M Frère, J Van Beeumen.
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.Entities:
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Year: 1987 PMID: 3307765 PMCID: PMC1147891 DOI: 10.1042/bj2430561
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857