PMID:3046483

Citation	Prince, A, Wood, MS, Cacalano, GS and Chin, NX (1988) Isolation and characterization of a penicillinase from Pseudomonas cepacia 249. Antimicrob. Agents Chemother. 32:838-43
Abstract	Pseudomonas cepacia has an inducible beta-lactamase which is responsible for its novel ability to catabolize beta-lactam compounds. The gene encoding this enzyme, penA, was cloned from a genomic library of P. cepacia 249 on the broad-host-range cosmid pLAFR. This separated the penA gene from the gene encoding a second beta-lactamase in P. cepacia 249. Expression of penA was inducible in an Escherichia coli host strain by low levels of penicillin. The 33,500-molecular-weight enzyme had penicillinase activity not inhibited by clavulanic acid or sulbactam and was highly active against piperacillin and azlocillin. In comparison with other inducible beta-lactamases produced by gram-negative organisms, the penA enzyme had many properties which were similar to those of the penicillinase produced by Alcaligenes faecalis. It was unlike the ampC-type cephalosporinase produced by Pseudomonas aeruginosa.
Links	PubMed PMC172292
Keywords	Cloning, Molecular; Culture Media; DNA, Bacterial/biosynthesis; Escherichia coli/enzymology; Escherichia coli/genetics; Molecular Weight; Penicillinase/analysis; Penicillinase/isolation & purification; Plasmids; Pseudomonas/enzymology; Pseudomonas/genetics
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
BURCE:O08350		GO:0033250: penicillinase activity	ECO:0000316:	PMID:6329713	F		table 3. Penicillinase activity in a strain of E. coli with no background penicillinase activity was observed upon introduction of a vector containing penA from P. cepacia.	complete CACAO 4915

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