An amino acid substitution that blocks the deacylation step in the enzyme mechanism of penicillin‐binding protein 5 of Escherichia coli

FEBS Letters

Spratt, Brian G.¹  Broome-Smith, Jenny¹ 

[1] Microbial Genetics Group, School of Biological Sciences, University of Sussex, Falmer, Brighton BN1 9QG, Sussex, England

关键词: Penicillin-binding protein;    DNA sequencing;    Mutant;    Acyl-enzyme;    Sulfhydryl reagent;    Escherichia coli;   

DOI  :  10.1016/0014-5793(84)80166-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown