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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Broome-Smith J,Spratt BG

doi

10.1016/0014-5793(84)80166-0

subject

Has Abstract

pub_date

1984-01-09 00:00:00

pages

185-9

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(84)80166-0

journal_volume

165

pub_type

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