1986
DOI: 10.1042/bj2340343
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Structural and kinetic studies on β-lactamase K1 from Klebsiella aerogenes

Abstract: beta-Lactamase K1 from Klebsiella aerogenes 1082E hydrolyses both penicillins and cephalosporins comparably and is inhibited by mercurials but not by cloxacillin. These properties distinguish it from those other beta-lactamases that have been allotted to classes on the basis of their amino sequences. beta-Lactamase K1 has been isolated by affinity chromatography; its composition shows resemblances to class A beta-lactamases. Moreover, the N-terminal sequence is similar to those of class A beta-lactamases: ther… Show more

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Cited by 16 publications
(17 citation statements)
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“…The high homology of nucleotide sequences between the&lactamase gene of K. pneumoniae LEN-l and the TEM ,&lactamase gene of Tn3 clearly shows that these two kinds of ,&-lactamases originate from a common ancestor and belong to class A. Our results based on the nucleotide sequence analysis are consistent with the recent finding by Emanuel et al [14] that the fl-lactamase of K. aerogenes (K. pneumoniae) related to class A fllactamases on the basis of the limited amino acid sequence analysis of the peptide. The relatively low homology in the 60 amino acid sequence from Nterminal and 20 amino acid from C-terminal (36 and 43% homology, respectively) suggests that these portions do not play essential roles in their enzymatic activities.…”
Section: Hybridizationsupporting
confidence: 92%
“…The high homology of nucleotide sequences between the&lactamase gene of K. pneumoniae LEN-l and the TEM ,&lactamase gene of Tn3 clearly shows that these two kinds of ,&-lactamases originate from a common ancestor and belong to class A. Our results based on the nucleotide sequence analysis are consistent with the recent finding by Emanuel et al [14] that the fl-lactamase of K. aerogenes (K. pneumoniae) related to class A fllactamases on the basis of the limited amino acid sequence analysis of the peptide. The relatively low homology in the 60 amino acid sequence from Nterminal and 20 amino acid from C-terminal (36 and 43% homology, respectively) suggests that these portions do not play essential roles in their enzymatic activities.…”
Section: Hybridizationsupporting
confidence: 92%
“…Similar situations are certain to arise in the future with enzymes that have not been examined by using the z Amino acid sequences of active-site peptides of K1 enzymes from 1082E and SC10436 differed only at the residue preceding the active site serine: asparagine in strain 1082E and cysteine in strain SC10436. Substitutions were compatible with differential susceptibilities to thiol group reagents (82,135).…”
Section: Discussionmentioning
confidence: 99%
“…K. oxytoca is naturally resistant to aminoand carboxy-penicillins (21), a phenotype due to the constitutive expression of a chromosomal class A ␤-lactamase (1), first called K1 (7,20) or KOXY (26) and now OXY (12). Due to the hyperproduction of the chromosomal ␤-lactamase, up to 10 to 20% of K. oxytoca strains (22) can show high-level resistance to certain expanded-spectrum cephalosporins (ceftriaxone and cefotaxime) and aztreonam (8).…”
mentioning
confidence: 99%