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

Author:

Tanaka Shuji1,Lerner Stephen A.1,Lin Edmund C. C.1

Affiliation:

1. 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.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

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