Kinase replacement by a dehydrogenase for Escherichia coli glycerol utilization

J Bacteriol. 1977 Sep;131(3):1026-8. doi: 10.1128/jb.131.3.1026-1028.1977.

Abstract

A mutant of Escherichia coli that employs a glycerol:nicotinamide adenine dinucleotide 2-oxidoreductase (EC 1.1.1.6), instead of adenosine 5'-triphosphate:glycerol 3-phosphotransferase (EC 2.7.1.30), as the first enzyme for the dissimilation of glycerol was constructed. This mutant, like the wild-type strain, still cannot grow anaerobically on glycerol without an exogenous hydrogen acceptor.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Aerobiosis
  • Alcohol Oxidoreductases / metabolism*
  • Escherichia coli / enzymology
  • Escherichia coli / growth & development
  • Escherichia coli / metabolism*
  • Glycerol / metabolism*
  • Glycerol Kinase / metabolism*
  • Mutation*
  • NAD / metabolism
  • Phosphotransferases / metabolism*

Substances

  • NAD
  • Alcohol Oxidoreductases
  • Phosphotransferases
  • Glycerol Kinase
  • Glycerol