Isolation of mutants of Escherichia coli lacking NAD- and NADP-linked malic enzyme activities

Eric J. Hansen, Elliot Juni

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

When Escherichia coli utilizes C4-dicarboxylic acids as sole sources of carbon and energy for growth, phosphoenolpyruvate is synthesized by means of phosphoenolpyruvate carboxykinase or by sequential action of malic enzyme and phosphoenolpyruvate synthetase. Chemical mutagenesis of a strain of E. coli K-12 lacking phosphoenolpyruvate carboxykinase activity yielded a mutant which grows very slowly on malate-mineral medium and lacks NAD-linked malic enzyme activity as well as phosphoenolpyruvate carboxykinase activity. A revertant of this double mutant which possesses elevated levels of NADP-linked malic enzyme activity grows well on malate-mineral medium. Further mutagenesis of this revertant produced a mutant which grows very slowly on malate-mineral medium and lacks NADP-linked malic enzyme activity as well as phosphoenolpyruvate carboxykinase and NAD-linked malic enzyme activities.

Original languageEnglish (US)
Pages (from-to)559-566
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume65
Issue number2
DOIs
StatePublished - Jul 22 1975

Fingerprint

malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)
Phosphoenolpyruvate
Enzyme activity
NADP
NAD
Escherichia coli
malate dehydrogenase-(oxaloacetate-decarboxylating) (NAD+)
Minerals
Mutagenesis
Dicarboxylic Acids
Ligases
Carbon
Enzymes
Growth

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Isolation of mutants of Escherichia coli lacking NAD- and NADP-linked malic enzyme activities. / Hansen, Eric J.; Juni, Elliot.

In: Biochemical and Biophysical Research Communications, Vol. 65, No. 2, 22.07.1975, p. 559-566.

Research output: Contribution to journalArticle

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