An amino acid substitution that blocks the deacylation step in the enzyme mechanism of penicillin-binding protein 5 of Escherichia coli.
FEBS Lett
; 165(2): 185-9, 1984 Jan 09.
Article
em En
| MEDLINE
| ID: mdl-6319180
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Muramilpentapeptídeo Carboxipeptidase
/
Proteínas de Transporte
/
Peptidil Transferases
/
Escherichia coli
/
Hexosiltransferases
/
Mutação
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
1984
Tipo de documento:
Article