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.
1. A spectrophotometric assay for thiogalactoside transacetylase;ALPERS D. H.;J. Biol. Chem.,1965
2. Proof of hybrid enzyme formation in a case of inter-allelic complementation in Neurospora crassa;CODDINGTON A.;J. Mol. Biol.,1965
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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