Carbenicillin-hydrolysing penicillinase mediated by a plasmid of Proteus mirabilis and its relationship to the PSE-type enzymes of Pseudomonas aeruginosa.
The nucleotide sequence of a carbenicillin-hydrolysing (carbenicillinase) gene occurring in an endogenous plasmid, pCS229, of Proteus mirabilis was determined. The amino acid sequence of the mature enzyme, comprising 271 amino acids with a molecular mass of 29,506 Da, was deduced. The pCS229 carbenicillinase showed only 46.4% similarity, in the overall amino acid sequence, to the chromosomal carbenicillinase of Pr. mirabilis GN79; however, the enzyme showed about 98% similarity to a Pseudomonas-specific plasmid-encoded carbenicillinase, PSE-4, that was isolated from Pseudomonas aeruginosa. Only five of 271 amino acids differed from those of PSE-4. This study proved the close relationship between the carbenicillinase genes distributed in Pr. mirabilis and Ps. aeruginosa.
Ito
Y
Y
Biomolecules Department, National Institute of Bioscience and Human Technology, Ibaraki, Japan.
Hirano
T
T
D000595:Amino Acid Sequence; D001483:Base Sequence; D017124:Conserved Sequence; D004926:Escherichia coli / Q000235:genetics; D015964:Gene Expression Regulation, Bacterial; D015971:Gene Expression Regulation, Enzymologic; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D010405:Penicillinase / Q000235:genetics*; D010957:Plasmids; D011513:Proteus mirabilis / Q000201:enzymology / Q000235:genetics*; D011550:Pseudomonas aeruginosa / Q000201:enzymology / Q000235:genetics*; D017386:Sequence Homology, Amino Acid
D010405:Penicillinase