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. 1967 Feb;93(2):642-8.
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 mannitol

S Tanaka, S A Lerner, E C Lin

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

S Tanaka et al. J Bacteriol. 1967 Feb.

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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