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- W2091217154 abstract "A mutant of Escherichia coli has been described that produces an altered form of penicillin-binding protein 5 which still binds penicillin but is unable to catalyse the release of the bound penicilloyl moiety. We show that the mutation is caused by a single nucleotide transition that results in a change from glycine at residue 105 of the wild-type sequence of penicillin-binding protein 5 to aspartate in the mutant." @default.
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- W2091217154 date "1984-01-09" @default.
- W2091217154 modified "2023-10-17" @default.
- W2091217154 title "An amino acid substitution that blocks the deacylation step in the enzyme mechanism of penicillin-binding protein 5 ofEscherichia coli" @default.
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- W2091217154 doi "https://doi.org/10.1016/0014-5793(84)80166-0" @default.
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