Mutants of Escherichia coli lacking in highly penicillin-sensitive D-alanine carboxypeptidase activity
| Autor: | Hideho Suzuki, Utako Ogino, Shigeo Tamaki, Ichiro N. Maruyama, Yukinobu Nishimura, Yohtaroh Takagaki, Michio Matsuhashi, Yukinori Hirota |
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| Rok vydání: | 1977 |
| Předmět: |
Mutant
Carboxypeptidases Peptidoglycan medicine.disease_cause chemistry.chemical_compound Escherichia coli medicine Alanine chemistry.chemical_classification Mutation Multidisciplinary biology Temperature Chromosome Mapping Penicillin G Carboxypeptidase Molecular biology Endopeptidase Enzyme Genes chemistry Biochemistry biology.protein Carrier Proteins Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 74:2976-2979 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.74.7.2976 |
| Popis: | 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 mutation results in the simultaneous loss of D-alanine carboxypeptidase and penicillin-binding protein 4. The mutants grew normally under a wide range of growth conditions. We conclude that the enzyme is not a necessary component for normal peptidoglycan biosynthesis in E. coli. |
| Databáze: | OpenAIRE |
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