Mutants of Escherichia coli lacking in highly penicillin-sensitive D-alanine carboxypeptidase activity.

@article{Matsuhashi1977MutantsOE,
  title={Mutants of Escherichia coli lacking in highly penicillin-sensitive D-alanine carboxypeptidase activity.},
  author={M. Matsuhashi and Yohtaroh Takagaki and Ichiro N. Maruyama and Shigeo Tamaki and Yosuke Nishimura and Hideho Suzuki and U Ogino and Yukinori Hirota},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1977},
  volume={74 7},
  pages={2976-9}
}
Mutants of Escherichia coli lacking in the highly penicillin-sensitive enzyme activities of D-carboxy-peptidase, transpeptidase, and endopeptidase, and with the concomitant absence of penicillin-binding protein 4 of B.G. Spratt and A.B. Pardee [(1975) Nature 254, 516-517] were isolated. The defect of these mutants is ascribed to the lack of an enzyme, D-alanine carboxypeptidase Ib. Genetic mapping studies show the mutation (dacB) to be located at 68 min on the E. coli chromosome map. The dacB… CONTINUE READING

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