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. 1969 Dec;100(3):1378–1384. doi: 10.1128/jb.100.3.1378-1384.1969

Pyrimidine Synthesis in Neurospora crassa: Regulation of Enzyme Activities

Dina F Caroline a,1, Rowland H Davis a
PMCID: PMC250345  PMID: 5361219

Abstract

The regulation of several enzymes involved in pyrimidine biosynthesis in Neurospora crassa has been studied. Elevation of ATCase (l-aspartate carbamoyltransferase) activity is found in all pyrimidine-requiring mutants when they are starved for uridine. DHOase (dihydroorotase) is an unstable enzyme, and it is impossible to conclude what type of regulation, if any, controls this enzyme. DHOdehase (dihydroorotate dehydrogenase) activity shows a marked elevation in uridine-starved pyr-2 cultures, a mutant blocked late in the pathway. Several mutants blocked early in the pathway show much smaller increases in DHOdehase activity and possible explanations for this are discussed. Differences in the modes of regulation of the pyrimidine biosynthetic pathways in various organisms are compared.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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