Regulation and function of glutamate synthase in Neurospora crassa

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Abstract

In Neurospora crassa two enzymes can provide glutamate: the NADPH dependent GDH and the NADH dependent GOGAT. An elevated GOGAT activity was found in Neurospora wild-type under ammonium limitation in contrast to a 4-fold lower activity on excess of am monium. Glutamate and glutamine repress this enzyme. On excess of ammonium the GDH-NADPH deficient mutant am-1 grows poorly with an elevated GOGAT activity. A GOGAT less mutant was found. It presented a lag-phase to grow on ammonium. It is concluded that N. crassa glutamate synthase provides glutamate from low am-monium concentrations. The enzyme was purified to homogeneity and shown to be composed of a single type of monomer with a molecular weight above 200,000.

References (14)

  • G. Hummelt et al.

    Biochem. Biophys. Res. Commun

    (1980)
  • G. Dávila et al.

    Biochem. Biophys. Res. Commun

    (1980)
  • F. Sánchez et al.

    J. Biol. Chem

    (1980)
  • J. Limón-Lason et al.

    Biochem. Biophys. Res. Commun

    (1977)
  • R.H. Davis et al.

    Genetic and microbiological research techniques for Neurospora crassa

    Methods Enzymol

    (1970)
  • O.H. Lowry et al.

    J. Biol. Chem

    (1951)
  • D.W. Tempest et al.

    Biochem. J

    (1970)
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