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

^a Department of Biological Chemistry, Harvard Medical School, Boston, Massachusetts

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.

² Present address: Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, Md.

³ Supported by a Research Career Development Award from the U.S. Public Health Service.

¹ Part of this work was presented before the American Society of Biological Chemists, Atlantic City, N.J., April, 1962 (Lerner and Lin, Federation Proc. 21:268, 1962).

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