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Article

Ferrioxamine transport mutants and the identification of the ferrioxamine receptor protein (FoxA) in Erwinia herbicola (Enterobacter agglomerans).

Biology of metals - 1 Jan 1990

Berner I, Winkelmann G

Abstract excerpt

Iron deprivation of Erwinia herbicola (Enterobacter agglomerans) induces the biosynthesis of six high-Mr outer-membrane proteins and large amounts of ferrioxamine E. Mutagenesis with N-methyl-N'-nitro-N-nitrosoguanidine and selection with ferrimycin A yielded mutants of E. herbicola K4 (wild type), defective in the expression of a 76-kDa outer-membrane protein, as determined by SDS/polyacrylamide gel...

Topics

Anti-Bacterial Agents
Bacterial Outer Membrane Proteins
Biological Transport, Active
Deferoxamine
Drug Resistance, Microbial
Erwinia
Ferric Compounds
Iron
Methylnitronitrosoguanidine
Molecular Structure

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Weight

Mutation

Organometallic Compounds

Source

Identifiers

PMID: 2390414
DOI: 10.1007/BF01141359

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SDS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2390414-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Ferrioxamine transport mutants and the identification of the ferrioxamine receptor protein (FoxA) in Erwinia herbicola (Enterobacter agglomerans).PMID 2390414Read ↗

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