A possible role in the regulation of primary amination for a complex of glutamine: α-Ketoglutarate amidotransferase and glutamate dehydrogenase in Escherichia coli

Michael A. Savageau, Ann Marie Kotre, Naoto Sakamoto

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Both glutamine: α-ketoglutarate amidotransferase and glutamate dehydrogenase activities are obtained from Escherichia coli grown in minimal medium containing glucose and ammonia. These activities are not additive, suggesting an interaction between them. Normally both of these activities are equally inhibited by homoserine. In mutants resistant to homoserine inhibition both activities are affected in parallel. Furthermore, the ratio of the wild-type activities remains constant over a 30-fold range in purification. This evidence suggests that these activities are associated with a single complex. A possible role for this complex in the regulation of primary amination is discussed.

Original languageEnglish (US)
Pages (from-to)41-47
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume48
Issue number1
DOIs
StatePublished - Jul 11 1972
Externally publishedYes

Fingerprint

Glutamate Synthase
Homoserine
Amination
Glutamate Dehydrogenase
Escherichia coli
Ammonia
Purification
Glucose

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

A possible role in the regulation of primary amination for a complex of glutamine : α-Ketoglutarate amidotransferase and glutamate dehydrogenase in Escherichia coli. / Savageau, Michael A.; Kotre, Ann Marie; Sakamoto, Naoto.

In: Biochemical and Biophysical Research Communications, Vol. 48, No. 1, 11.07.1972, p. 41-47.

Research output: Contribution to journalArticle

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