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. 1972 Dec;112(3):1142–1149. doi: 10.1128/jb.112.3.1142-1149.1972

Enterochelin System of Iron Transport in Escherichia coli: Mutations Affecting Ferric-Enterochelin Esterase

Lyndall Langman 1, I G Young 1, G E Frost 1, H Rosenberg 1, F Gibson 1
PMCID: PMC251542  PMID: 4565531

Abstract

Three mutant strains of Escherichia coli have been isolated which are lacking ferric-enterochelin esterase activity. This enzyme catalyzes the hydrolysis of the enterochelin moiety of ferric-enterochelin to yield ultimately three molecules of N-2,3-dihydroxybenzoylserine. The mutants (designated fes−) were shown to be unaffected in enterochelin biosynthesis, capable of enterochelin-mediated iron uptake, and able to utilize ferric-dihydroxybenzoylserine complexes normally. When grown under iron-deficient conditions, however, they showed an absolute requirement for added iron or citrate, a phenotype characteristic of mutants defective in some part of the enterochelin system of iron uptake. These results support the theory that iron, taken up by the cell as ferric-enterochelin is only available for general cell metabolism after hydrolysis of the ligand by enterochelin esterase. The three fes− strains were shown to be affected in the B component of enterochelin esterase. The fesB gene which is probably the structural gene coding for component B of the esterase, was shown to be located at about minute 14 on the E. coli chromosome together with seven other genes involved in the enterochelin system of iron transport.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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