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PMID: 6319180 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

FEBS letters ·Vol. 165 ·No. 2 ·1984-01-09 ·Pages 185-9

Broome-Smith J, Spratt BG

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.

MeSH Terms

Acylation Amino Acid Sequence Bacterial Proteins Base Sequence Carrier Proteins/genetics,metabolism DNA Restriction Enzymes DNA, Bacterial/genetics Escherichia coli/enzymology,genetics Hexosyltransferases Muramoylpentapeptide Carboxypeptidase Mutation Penicillin G/metabolism Penicillin-Binding Proteins Peptidyl Transferases Structure-Activity Relationship

Chemicals

Bacterial Proteins Carrier Proteins DNA, Bacterial Penicillin-Binding Proteins Peptidyl Transferases Hexosyltransferases DNA Restriction Enzymes Muramoylpentapeptide Carboxypeptidase Penicillin G

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Broome-Smith J

Spratt B G

Article Info

Journal

FEBS letters

Abbr.

FEBS Lett

ISSN

0014-5793

DOI

10.1016/0014-5793(84)80166-0

Published

1984-01-09

Pages

185-9

Language

English

Region

England

NLM ID

0155157

Subset

Databases

GENBANK

X00273, X06479

External Links

PubMed source DOI: 10.1016/0014-5793(84)80166-0 View journal details

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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.

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