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. 1986 Mar;165(3):710–714. doi: 10.1128/jb.165.3.710-714.1986

Isolation of a mutation resulting in constitutive synthesis of L-fucose catabolic enzymes.

J M Bartkus, R P Mortlock
PMCID: PMC214487  PMID: 3005235

Abstract

A ribitol-positive transductant of Escherichia coli K-12, JM2112, was used to facilitate the isolation and identification of mutations affecting the L-fucose catabolic pathway. Analysis of L-fucose-negative mutants of JM2112 enabled us to confirm that L-fucose-1-phosphate is the apparent inducer of the fucose catabolic enzymes. Plating of an L-fuculokinase-negative mutant of JM2112 on D-arabinose yielded an isolate containing a second fucose mutation which resulted in the constitutive synthesis of L-fucose permease, isomerase, and kinase. This constitutive mutation differs from the constitutive mutation described by Chen et al. (J. Bacteriol. 159:725-729, 1984) in that it is tightly linked to the fucose genes and appears to be located in the gene believed to code for the positive activator of the L-fucose genes.

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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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