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An amino acid substitution that blocks the deacylation step in the enzyme mechanism of penicillin‐binding protein 5 of Escherichia coli
Author(s) -
Broome-Smith Jenny,
Spratt Brian G.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80166-0
Subject(s) - escherichia coli , mutant , biochemistry , penicillin binding proteins , chemistry , residue (chemistry) , penicillin , nucleotide , enzyme , amino acid , moiety , binding site , mutation , glycine , stereochemistry , antibiotics , gene
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.