Nucleotide sequence and characterization of a carbenicillin-hydrolyzing penicillinase gene from Proteus mirabilis.
The structural gene of a carbenicillinase was cloned from the chromosomal DNA of Proteus mirabilis GN79. This gene codes for a protein of 270 amino acids. Alignment of the amino acid sequence with those of known beta-lactamases revealed that the enzyme is a novel class A beta-lactamase with a unique conserved triad, RTG. By using a DNA fragment of the structural gene, a lack of cross hybridization was confirmed between the DNA probe and total DNAs from natural isolates of P. mirabilis, suggesting that the carbenicillinase may not be a species-specific beta-lactamase of P. mirabilis.
Sakurai
Y
Y
Division of Microbial Chemistry, Faculty of Pharmaceutical Sciences, Chiba University, Japan.
Tsukamoto
K
K
Sawai
T
T
D000595:Amino Acid Sequence; D001483:Base Sequence; D002228:Carbenicillin / Q000378:metabolism*; D003001:Cloning, Molecular; D004269:DNA, Bacterial; D006868:Hydrolysis; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D010405:Penicillinase / Q000235:genetics* / Q000378:metabolism; D011513:Proteus mirabilis / Q000201:enzymology / Q000235:genetics*; D016415:Sequence Alignment
D004269:DNA, Bacterial; D010405:Penicillinase; D002228:Carbenicillin