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Journal of Bacteriology logoLink to Journal of Bacteriology
. 1967 Feb;93(2):642–648. doi: 10.1128/jb.93.2.642-648.1967

Replacement of a Phosphoenolpyruvate-dependent Phosphotransferase by a Nicotinamide Adenine Dinucleotide-linked Dehydrogenase for the Utilization of Mannitol1

Shuji Tanaka a, Stephen A Lerner a,2, Edmund C C Lin a,3
PMCID: PMC276489  PMID: 4289962

Abstract

Mannitol is dissimilated by Aerobacter aerogenes via an inducible pathway initiated by a phosphotransferase system dependent upon phosphoenolpyruvate as the phosphoryl donor. A mutational block in this pathway can be suppressed either at the phenotypic level by induction of d-arabitol dehydrogenase, an enzyme fortuitously capable of converting mannitol to fructose, or genotypically by a constitutive mutation in the d-arabitol system.

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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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