Acetate-nonutilizing Mutants of Neurospora crassa II. Biochemical Deficiencies and the Roles of Certain Enzymes

Author:

Flavell R. B.1,Fincham J. R. S.2

Affiliation:

1. The John Innes Institute, Bayfordbury, Herts., England

2. Department of Genetics, The University, Leeds, England

Abstract

The levels of Krebs cycle, glyoxylate cycle, and certain other enzymes were measured in a wild-type strain and in seven groups of acetate-nonutilizing ( acu ) mutants of Neurospora crassa , both after growth on a medium containing sucrose and after a subsequent 6-hr incubation in a similar medium, containing acetate as the sole source of carbon. In the wild strain, incubation in acetate medium caused a rise in the levels of isocitrate lyase, malate synthase, phosphoenolpyruvate carboxykinase, acetyl-coenzyme A synthetase, nicotinamide adenine dinucleotide phosphate-linked isocitrate dehydrogenase, citrate synthase, and fumarate hydratase. Isocitrate lyase activity was absent in acu-3 mutants; acu-5 mutants lacked acetyl-coenzyme A synthetase activity; and no oxoglutarate dehydrogenase activity (or only low levels) could be detected in acu-2 and acu-7 mutants. In acu-6 mutants, phosphoenolpyruvate carboxykinase activity was either very low or absent. No specific biochemical deficiencies could be attributed to the acu-1 and acu-4 mutations. The role of several of these enzymes during growth on acetate is discussed.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference26 articles.

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3. Assay methods for key enzymes of the glyoxylate cycle;DIXON S. H.;Biochem. J.,1959

4. Mutant strains of Neurospora deficient in aminating ability;FINCHAM J. R.;J. Biol. Chem.,1950

5. 1068 FLAVELL AND FINCHAM

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