Replacement of a phosphoenolpyruvate-dependent phosphotransferase by a nicotinamide adenine dinucleotide-linked dehydrogenase for the utilization of mannitol.

@article{Tanaka1967ReplacementOA,
  title={Replacement of a phosphoenolpyruvate-dependent phosphotransferase by a nicotinamide adenine dinucleotide-linked dehydrogenase for the utilization of mannitol.},
  author={Seiichi Tanaka and Stephen A. Lerner and E. C. Lin},
  journal={Journal of bacteriology},
  year={1967},
  volume={93 2},
  pages={642-8}
}
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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